The peculiar structural features of kiwi fruit pectin methylesterase: Amino acid sequence, oligosaccharides structure, and modeling of the interaction with its natural proteinaceous inhibitor

2008 ◽  
Vol 71 (1) ◽  
pp. 195-206 ◽  
Author(s):  
M. Antonietta Ciardiello ◽  
Rossana D'Avino ◽  
Angela Amoresano ◽  
Lisa Tuppo ◽  
Andrea Carpentieri ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Pectin Methylesterase ◽  
Structural Features ◽  
Kiwi Fruit ◽  
Proteinaceous Inhibitor

scholarly journals Structural features of the low-molecular-mass human salivary mucin

1992 ◽  
Vol 287 (2) ◽  
pp. 639-643 ◽  
Author(s):  
M S Reddy ◽  
L A Bobek ◽  
G G Haraszthy ◽  
A R Biesbrock ◽  
M J Levine
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Molecular Mass ◽  
Gel Filtration ◽  
Structural Features ◽  
Cdna Expression Library ◽  
Cdna Clones ◽  
Expression Library ◽  
Mrna Species ◽  
Salivary Mucin

The low-molecular-mass human salivary mucin has at least two isoforms, MG2a and MG2b, that differ primarily in their sialic acid and fucose content. In this study, we characterize further these isoforms, particularly their peptide moieties. Trypsin digests of MG2a and MG2b yielded high- and low-molecular-mass glycopeptides following gel filtration on Sephacryl S-300. The larger glycopeptides from MG2a and MG2b had similar amino acid compositions and identical N-terminal sequences, suggesting common structural features between their peptides. An oligonucleotide probe generated from the amino acid sequence of the smaller glycopeptide from MG2a was employed in Northern-blot analysis. This probe specifically hybridized to two mRNA species from human submandibular and sublingual glands. A cDNA clone selected from a human submandibular gland cDNA expression library with antibody generated against deglycosylated MG2a also hybridized to these two mRNA species. In both cases, the larger mRNA was polydisperse, and the hybridization signal was more intense in the sublingual gland. In addition, the N-terminal amino acid sequence of the larger glycopeptide was found to be part of one of the selected MG2 cDNA clones.

Crystal structure of hemoglobin from mouse (Mus musculus) compared with those from other small animals and humans

2021 ◽  
Vol 77 (4) ◽  
pp. 113-120
Author(s):  
Selvarajan Sigamani Sundaresan ◽  
Pandian Ramesh ◽  
Nagaraj Shobana ◽  
Thangaraj Vinuchakkaravarthy ◽  
Sayed Yasien ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Mus Musculus ◽  
Structural Features ◽  
Small Animals ◽  
Orthorhombic Space Group ◽  
Primary Amino ◽  
The Difference ◽  
Function Relationship

Mice (Mus musculus) are nocturnal small animals belonging to the rodent family that live in burrows, an environment in which significantly high CO2 levels prevail. It is expected that mouse hemoglobin (Hb) plays an important role in their adaptation to living in such a high-CO2 environment, while many other species cannot. In the present study, mouse Hb was purified and crystallized at a physiological pH of 7 in the orthorhombic space group P212121; the crystals diffracted to 2.8 Å resolution. The primary amino-acid sequence and crystal structure of mouse Hb were compared with those of mammalian Hbs in order to investigate the structure–function relationship of mouse Hb. Differences were observed from guinea pig Hb in terms of amino-acid sequence and from cat Hb in overall structure (in terms of r.m.s.d.). The difference in r.m.s.d. from cat Hb may be due to the existence of the molecule in a conformation other than the R-state. Analysis of tertiary- and quaternary-structural features, the α1β2 interface region and the heme environment without any ligands in all four heme groups showed that mouse methemoglobin is in an intermediate state between the R-state and the T-state that is much closer to the R-state conformation.

scholarly journals Amino Acid Sequence Studies on the γ-Chain of Human Fibrinogen

1977 ◽  
Author(s):  
H. Bouma ◽  
B. A. Cottrell ◽  
S. J. Friezner ◽  
T. Takagi ◽  
R. F. Doolittle
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cyanogen Bromide ◽  
Sequence Data ◽  
Structural Features ◽  
Tryptic Digestion ◽  
Cysteine Residues ◽  
Human Fibrinogen

The γ-chain of human fibrinogen contains 400±10 residues, eight of which are methionines. As such, we have isolated and characterized nine cyanogen bromide peptides. The alignment of these fragments was attained by the isolation of key overlap peptides derived from the tryptic digestion of citraconylated γ-chains and succinylated and aminoethylated γ-chains. In the latter case we synthesized a radioactive aminoethylating agent which was especially useful in isolating all the cysteine-containing peptides. The amino acid sequence of most of these fragments has been accomplished by a variety of procedures. In general, our results are in harmony with those recently reported by Henschen et al. (Hoppe-Seyler’s Z. Physiol. Chem., 357, 605, 1976), although some differences exist.The most interesting structural features revealed by the sequence data include significant homologies with the α- and β-chains, especially with regard to the arrangement of certain key cysteine residues. Thus, the sequence at residues γ 135–139 is Cys-Gln-Glu-Pro-Cys, in striking parallel with the sequence at residues γ 19–23, which is Cys-Pro-Thr-Thr-Cys. The occurrence of similar pentapeptide skeins in the α- and β-chains, in each case separated by about the same number of residues, has both structural and evolutionary connotations.

scholarly journals A 3.8 Å Resolution Cryo-EM Structure of a Small Protein Bound to a Modular Imaging Scaffold

2018 ◽  
Author(s):  
Yuxi Liu ◽  
Duc Huynh ◽  
Todd O Yeates
Keyword(s):  
Electron Microscopy ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Structural Features ◽  
Cryo Electron Microscopy ◽  
Cargo Protein ◽  
Size Limitation ◽  
Protein Molecules ◽  
Lower Size ◽  
General Method

Proteins smaller than about 50 kDa are currently too small to be imaged by cryo-electron microscopy (cryo-EM), leaving most protein molecules in the cell beyond the reach of this powerful structural technique. Here we use a designed protein scaffold to bind and symmetrically display 12 copies of a small 26 kDa protein. We show that the bound cargo protein is held rigidly enough to visualize it at a resolution of 3.8 Å by cryo-EM, where basic structural features of the protein are visible. The designed scaffold is modular and can be modified through modest changes in its amino acid sequence to bind and display diverse proteins for imaging, thus providing a general method to break through the lower size limitation in cryo-EM.

Effect of Intrinsic and Extrinsic Factors on the Interaction of Plant Pectin Methylesterase and Its Proteinaceous Inhibitor from Kiwi Fruit

2004 ◽  
Vol 52 (26) ◽  
pp. 8144-8150 ◽  
Author(s):  
Binh Ly-Nguyen ◽  
Ann M. Van Loey ◽  
Chantal Smout ◽  
Isabel Verlent ◽  
Thomas Duvetter ◽  
...  
Keyword(s):  
Pectin Methylesterase ◽  
Extrinsic Factors ◽  
Kiwi Fruit ◽  
Proteinaceous Inhibitor ◽  
Intrinsic And Extrinsic Factors

The staining pattern of the tropomyosin sequence is displayed in a new paracrystal

1986 ◽  
Vol 44 ◽  
pp. 150-151
Author(s):  
M.K. Lamvik ◽  
L.L. Klatt
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Staining Pattern ◽  
Banding Patterns ◽  
Mass Thickness ◽  
New Form

Tropomyosin paracrystals have been used extensively as test specimens and magnification standards due to their clear periodic banding patterns. The paracrystal type discovered by Ohtsuki1 has been of particular interest as a test of unstained specimens because of alternating bands that differ by 50% in mass thickness. While producing specimens of this type, we came across a new paracrystal form. Since this new form displays aligned tropomyosin molecules without the overlaps that are characteristic of the Ohtsuki-type paracrystal, it presents a staining pattern that corresponds to the amino acid sequence of the molecule.

Isolation and Structural Charaderization of a Potent Inhibitor of Coagulation Factor Xa from the Leech Haementeria ghilianii

1989 ◽  
Vol 61 (03) ◽  
pp. 437-441 ◽  
Author(s):  
Cindra Condra ◽  
Elka Nutt ◽  
Christopher J Petroski ◽  
Ellen Simpson ◽  
P A Friedman ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Salivary Gland ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Western Blot ◽  
Potent Inhibitor ◽  
Factor Xa ◽  
Coagulation Factor ◽  
Sds Page ◽  
Bovine Factor

SummaryThe present work reports the discovery and charactenzation of an anticoagulant protein in the salivary gland of the giant bloodsucking leech, H. ghilianii, which is a specific and potent inhibitor of coagulation factor Xa. The inhibitor, purified to homogeneity, displayed subnanomolar inhibition of bovine factor Xa and had a molecular weight of approximately 15,000 as deduced by denaturing SDS-PAGE. The amino acid sequence of the first 43 residues of the H. ghilianii derived inhibitor displayed a striking homology to antistasin, the recently described subnanomolar inhibitor of factor Xa isolated from the Mexican leech, H. officinalis. Antisera prepared to antistasin cross-reacted with the H. ghilianii protein in Western Blot analysis. These data indicate that the giant Amazonian leech, H. ghilianii, and the smaller Mexican leech, H. officinalrs, have similar proteins which disrupt the normal hemostatic clotting mechanisms in their mammalian host’s blood.

Paris I Dysfibrinogenemia: A Point Mutation in Intron 8 Results in Insertion of a 15 Amino Acid Sequence in the Fibrinogen γ-Chain

1993 ◽  
Vol 69 (03) ◽  
pp. 217-220 ◽  
Author(s):  
Jonathan B Rosenberg ◽  
Peter J Newman ◽  
Michael W Mosesson ◽  
Marie-Claude Guillin ◽  
David L Amrani
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Point Mutation ◽  
Genomic Dna ◽  
Comparative Sequence Analysis ◽  
Chain Gene ◽  
Molecular Defect ◽  
Nucleotide Position ◽  
Normal Individuals ◽  
Polymerase Chain

SummaryParis I dysfibrinogenemia results in the production of a fibrinogen molecule containing a functionally abnormal γ-chain. We determined the basis of the molecular defect using polymerase chain reaction (PCR) to amplify the γ-chain region of the Paris I subject’s genomic DNA. Comparative sequence analysis of cloned PCR segments of normal and Paris I genomic DNA revealed only an A→G point mutation occurring at nucleotide position 6588 within intron 8 of the Paris I γ-chain gene. We examined six normal individuals and found only normal sequence in this region, indicating that this change is not likely to represent a normal polymorphism. This nucleotide change leads to a 45 bp fragment being inserted between exons 8 and 9 in the mature γparis I chain mRNA, and encodes a 15 amino acid insert after γ350 [M-C-G-E-A-L-P-M-L-K-D-P-C-Y]. Alternative splicing of this region from intron 8 into the mature Paris I γ-chain mRNA also results after translation into a substitution of S for G at position γ351. Biochemical studies of 14C-iodoacetamide incorporation into disulfide-reduced Paris I and normal fibrinogen corroborated the molecular biologic predictions that two additional cysteine residues exist within the γpariS I chain. We conclude that the insertion of this amino acid sequence leads to a conformationallyaltered, and dysfunctional γ-chain in Paris I fibrinogen.

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