Three-Dimensional Structure of Leucocin A in Trifluoroethanol and Dodecylphosphocholine Micelles:  Spatial Location of Residues Critical for Biological Activity in Type IIa Bacteriocins from Lactic Acid Bacteria†,‡

Biochemistry ◽  
1997 ◽  
Vol 36 (49) ◽  
pp. 15062-15072 ◽  
Author(s):  
Nancy L. Fregeau Gallagher ◽  
Miloslav Sailer ◽  
Walter P. Niemczura ◽  
Thomas T. Nakashima ◽  
Michael E. Stiles ◽  
...  
Keyword(s):  
Biological Activity ◽  
Lactic Acid ◽  
Lactic Acid Bacteria ◽  
Three Dimensional ◽  
Spatial Location ◽  
Dimensional Structure ◽  
Three Dimensional Structure ◽  
Leucocin A

scholarly journals Three-dimensional structure modeling of a protease from lactic acid bacteria Leuconostoc mesenteroides K7 using automated protein homology analysis

2020 ◽  
Vol 21 (7) ◽  
Author(s):  
Habibi HIdayat ◽  
Winarto Haryadi ◽  
TRI JOKO RAHARJO
Keyword(s):  
Lactic Acid ◽  
Amino Acid ◽  
Lactic Acid Bacteria ◽  
Amino Acid Sequence ◽  
Leuconostoc Mesenteroides ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Structure Modeling ◽  
Protein Homology ◽  
Pcr Product

Abstract. Hidayat H, Haryadi W, Raharjo TJ. 2020. Three-dimensional structure modeling of a protease from lactic acid bacteria Leuconostoc mesenteroides K7 using automated protein homology analysis. Biodiversitas 21: 3156-3162. This study aimed to characterize the protease encoding gene of Leuconostoc mesenteroides K7 isolated from Kelengkeng (Dimocarpus longan) fruit as well as to predict the structure of the protein using in silico approach. Gene characterization was performed using PCR employs primers designed based on protease gene of other Leuconostoc species, followed by cloning and sequencing of the PCR product. Protein structural modeling was targeted to the deduced amino acid sequence of the gene employ multiple sequence alignment and SWISS-Model online software.  As a result, the sequence of the PCR product contains an open reading frame with a size of 1,140 bp, which can be translated into 379 amino acids. The amino acid sequence shares 98.60% identity with protease from Leuconostoc suionicum (AP017935.1). Three conserved sequences of QTDA, INPGNSGGPL, and FAIP are known as the signature from the Serine endoprotease DegS family are detected.  The three-dimensional modeling structure application shows that the protein share similarity of 37.62% to Protease Do-like I chloroplastic that belong to serine protease.

Biological activity and three-dimensional structure of an agonist analog of bombesin

2009 ◽  
Vol 51 (1) ◽  
pp. 55-64 ◽  
Author(s):  
ERIC CONDAMINE ◽  
GUILLAUME CHAPDELEINE ◽  
LYDIE DEMARCY ◽  
JEAN-FRANCOIS DUCLOS ◽  
DANIEL DAVOUST ◽  
...  
Keyword(s):  
Biological Activity ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Three Dimensional Structure

Substitution of a Conserved Disulfide in the Type IIa Bacteriocin, Leucocin A, with L-Leucine and L-Serine Residues: Effects on Activity and Three-Dimensional Structure

ChemBioChem ◽  
2011 ◽  
Vol 13 (1) ◽  
pp. 35-38 ◽  
Author(s):  
Clarissa S. Sit ◽  
Christopher T. Lohans ◽  
Marco J. van Belkum ◽  
Chantel D. Campbell ◽  
Mark Miskolzie ◽  
...  
Keyword(s):  
Three Dimensional ◽  
Dimensional Structure ◽  
Three Dimensional Structure ◽  
Leucocin A

The Three-dimensional structure of frozen-hydrated nudaurelia capensis β virus

1987 ◽  
Vol 45 ◽  
pp. 650-651
Author(s):  
N. H. Olson ◽  
T. S. Baker ◽  
Wu Bo Mu ◽  
J. E. Johnson ◽  
D. A. Hendry
Keyword(s):  
South African ◽  
Rna Virus ◽  
Carbon Film ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Electron Dose ◽  
Total Electron ◽  
Three Dimensional Structure ◽  
Negative Stain ◽  
Dimensional Reconstruction

Nudaurelia capensis β virus (NβV) is an RNA virus of the South African Pine Emperor moth, Nudaurelia cytherea capensis (Lepidoptera: Saturniidae). The NβV capsid is a T = 4 icosahedron that contains 60T = 240 subunits of the coat protein (Mr = 61,000). A three-dimensional reconstruction of the NβV capsid was previously computed from visions embedded in negative stain suspended over holes in a carbon film. We have re-examined the three-dimensional structure of NβV, using cryo-microscopy to examine the native, unstained structure of the virion and to provide a initial phasing model for high-resolution x-ray crystallographic studiesNβV was purified and prepared for cryo-microscopy as described. Micrographs were recorded ∼1 - 2 μm underfocus at a magnification of 49,000X with a total electron dose of about 1800 e-/nm2.

Three Dimensional structure and organization of diploid chromosomes by optical section microscopy

1987 ◽  
Vol 45 ◽  
pp. 633-635
Author(s):  
David A. Agard ◽  
Yasushi Hiraoka ◽  
John W. Sedat
Keyword(s):  
Dimensional Space ◽  
Three Dimensional ◽  
Developmental State ◽  
Mitotic Cell ◽  
Biological Properties ◽  
Dimensional Structure ◽  
Specific Gene ◽  
Three Dimensional Structure ◽  
Complementary Techniques ◽  
Dynamic Structures

In an effort to understand the complex relationship between structure and biological function within the nucleus, we have embarked on a program to examine the three-dimensional structure and organization of Drosophila melanogaster embryonic chromosomes. Our overall goal is to determine how DNA and proteins are organized into complex and highly dynamic structures (chromosomes) and how these chromosomes are arranged in three dimensional space within the cell nucleus. Futher, we hope to be able to correlate structual data with such fundamental biological properties as stage in the mitotic cell cycle, developmental state and transcription at specific gene loci.Towards this end, we have been developing methodologies for the three-dimensional analysis of non-crystalline biological specimens using optical and electron microscopy. We feel that the combination of these two complementary techniques allows an unprecedented look at the structural organization of cellular components ranging in size from 100A to 100 microns.

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