scholarly journals Crystal Structure of an Active Form of Monomeric Cytochrome c Oxidase from Bovine Heart

2020 ◽  
Vol 60 (5) ◽  
pp. 276-279
Author(s):  
Kyoko SHINZAWA-ITOH ◽  
Kazumasa MURAMOTO
Keyword(s):  
Crystal Structure ◽  
Active Form ◽  
Bovine Heart

scholarly journals Crystal structure of an active form of RAS protein, a complex of a GTP analog and the HRAS p21 catalytic domain.

1990 ◽  
Vol 87 (12) ◽  
pp. 4849-4853 ◽  
Author(s):  
A. T. Brunger ◽  
M. V. Milburn ◽  
L. Tong ◽  
A. M. deVos ◽  
J. Jancarik ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Catalytic Domain ◽  
Active Form ◽  
Protein A ◽  
Ras Protein

scholarly journals Latent and activeabPPO4 mushroom tyrosinase cocrystallized with hexatungstotellurate(VI) in a single crystal

2014 ◽  
Vol 70 (9) ◽  
pp. 2301-2315 ◽  
Author(s):  
Stephan Gerhard Mauracher ◽  
Christian Molitor ◽  
Rami Al-Oweini ◽  
Ulrich Kortz ◽  
Annette Rompel
Keyword(s):  
Crystal Structure ◽  
Single Crystal ◽  
Agaricus Bisporus ◽  
Crystal Packing ◽  
Active Form ◽  
Activation Mechanism ◽  
Mushroom Tyrosinase ◽  
Polyphenol Oxidases ◽  
Highly Active ◽  
Eukaryotic Organisms

Tyrosinases, bifunctional metalloenzymes, catalyze the oxidation of monophenols ando-diphenols too-quinones, the precursor compounds of the brown-coloured pigment melanin. In eukaryotic organisms, tyrosinases are expressed as latent zymogens that have to be proteolytically cleaved in order to form highly active enzymes. This activation mechanism, known as the tyrosinase maturation process, has scientific and industrial significance with respect to biochemical and technical applications of the enzyme. Here, not only the first crystal structure of the mushroom tyrosinaseabPPO4 is presented in its active form (Ser2–Ser383) and in its 21 kDa heavier latent form (Ser2–Thr545), but furthermore the simultaneous presence of both forms within one single-crystal structure is shown. This allows for a simple approach to investigate the transition between these two forms. IsoformabPPO4 was isolated and extensively purified from the natural source (Agaricus bisporus), which contains a total of six polyphenol oxidases (PPOs). The enzyme formed crystals (diffracting to a resolution of 2.76 Å) owing to the employment of the 6-tungstotellurate(VI) salt (Na6[TeW6O24]·22H2O) as a cocrystallization agent. Two of these disc-shaped Anderson-type polyoxoanions [TeW6O24]6−separate two asymmetric units comprising one crystallographic heterodimer ofabPPO4, thus resulting in very interesting crystal packing.

Crystal Structure of the Cytochrome bc1Complex from Bovine Heart Mitochondria

Science ◽  
1997 ◽  
Vol 277 (5322) ◽  
pp. 60-66 ◽  
Author(s):  
Di Xia ◽  
Chang-An Yu ◽  
Hoeon Kim ◽  
Jia-Zhi Xia ◽  
Anatoly M. Kachurin ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Heart Mitochondria ◽  
Bovine Heart

Crystal Structure of Bovine Heart Phosphotyrosyl Phosphatase at 2.2-.ANG. Resolution

Biochemistry ◽  
1994 ◽  
Vol 33 (37) ◽  
pp. 11097-11105 ◽  
Author(s):  
Marie Zhang ◽  
Robert L. Van Etten ◽  
Cynthia V. Stauffacher
Keyword(s):  
Crystal Structure ◽  
Bovine Heart

scholarly journals The Crystal Structure of the Active Form of the C-Terminal Kinase Domain of Mitogen- and Stress-Activated Protein Kinase 1

2010 ◽  
Vol 399 (1) ◽  
pp. 41-52 ◽  
Author(s):  
Margarita Malakhova ◽  
Igor D'Angelo ◽  
Hong-Gyum Kim ◽  
Igor Kurinov ◽  
Ann M. Bode ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Protein Kinase ◽  
Active Form ◽  
Kinase Domain

scholarly journals Crystal structure of wild-type human thrombin in the Na+-free state

2005 ◽  
Vol 392 (1) ◽  
pp. 21-28 ◽  
Author(s):  
Daniel J. D. Johnson ◽  
Ty E. Adams ◽  
Wei Li ◽  
James A. Huntington
Keyword(s):  
Crystal Structure ◽  
Protein C ◽  
Active Form ◽  
Bound State ◽  
Free Form ◽  
Wild Type ◽  
Thrombin Activity ◽  
Solution Studies ◽  
Human Thrombin ◽  
Anticoagulant Function

Regulation of thrombin activity is critical for haemostasis and the prevention of thrombosis. Thrombin has several procoagulant substrates, including fibrinogen and platelet receptors, and essential cofactors for stimulating its own formation. However, thrombin is also capable of serving an anticoagulant function by activating protein C. The specificity of thrombin is primarily regulated by binding to the cofactor TM (thrombomodulin), but co-ordination of Na+ can also affect thrombin activity. The Na+-free form is often referred to as ‘slow’ because of reduced rates of cleavage of procoagulant substrates, but the slow form is still capable of rapid activation of protein C in the presence of TM. The molecular basis of the slow proteolytic activity of thrombin has remained elusive, in spite of two decades of solution studies and many published crystallographic structures. In the present paper, we report the first structure of wild-type unliganded human thrombin grown in the absence of co-ordinating Na+. The Na+-binding site is observed in a highly ordered position 6 Å (1 Å=0.1 nm) removed from that seen in the Na+-bound state. The movement of the Na+ loop results in non-catalytic hydrogen-bonding in the active site and blocking of the S1 and S2 substrate-binding pockets. Similar, if more dramatic, changes were observed in a previous structure of the constitutively slow thrombin variant E217K. The slow behaviour of thrombin in solutions devoid of Na+ can now be understood in terms of an equilibrium between an inert species, represented by the crystal structure described in the present paper, and an active form, where the addition of Na+ populates the active state.

scholarly journals Crystal Structure of an ATPase-active Form of Rad51 Homolog fromMethanococcus voltae

2004 ◽  
Vol 280 (1) ◽  
pp. 722-728 ◽  
Author(s):  
Yan Wu ◽  
Xinguo Qian ◽  
Yujiong He ◽  
Ignace A. Moya ◽  
Yu Luo
Keyword(s):  
Crystal Structure ◽  
Active Form

scholarly journals Crystal Structure of an Active Form of BACE1, an Enzyme Responsible for Amyloid β Protein Production

2008 ◽  
Vol 28 (11) ◽  
pp. 3663-3671 ◽  
Author(s):  
Hideaki Shimizu ◽  
Asako Tosaki ◽  
Kumi Kaneko ◽  
Tamao Hisano ◽  
Takashi Sakurai ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Active Form ◽  
Amyloid Β ◽  
Bound Water ◽  
Structural Features ◽  
Cellular Trafficking ◽  
Amyloid Β Peptide ◽  
Amyloid Β Protein ◽  
Catalytically Active ◽  
Bace1 Activity

ABSTRACT BACE1 (β-secretase) is a transmembrane aspartic protease that cleaves the β-amyloid precursor protein and generates the amyloid β peptide (Aβ). BACE1 cycles between the cell surface and the endosomal system many times and becomes activated interconvertibly during its cellular trafficking, leading to the production of Aβ. Here we report the crystal structure of the catalytically active form of BACE1. The active form has novel structural features involving the conformation of the flap and subsites that promote substrate binding. The functionally essential residues and water molecules are well defined and play a key role in the iterative activation of BACE1. We further describe the crystal structure of the dehydrated form of BACE1, showing that BACE1 activity is dependent on the dynamics of a catalytically required Asp-bound water molecule, which directly affects its catalytic properties. These findings provide insight into a novel regulation of BACE1 activity and elucidate how BACE1 modulates its activity during cellular trafficking.

scholarly journals Crystal structure ofPorphyromonas gingivalispeptidylarginine deiminase: implications for autoimmunity in rheumatoid arthritis

2015 ◽  
Vol 75 (6) ◽  
pp. 1255-1261 ◽  
Author(s):  
Anna B Montgomery ◽  
Jolanta Kopec ◽  
Leela Shrestha ◽  
Marie-Laetitia Thezenas ◽  
Nicola A Burgess-Brown ◽  
...  
Keyword(s):  
Rheumatoid Arthritis ◽  
Crystal Structure ◽  
Active Form ◽  
3D Structure ◽  
Periodontal Pathogen ◽  
3D Structures ◽  
Highly Active ◽  
Lack Of Information ◽  
Arginine Residues ◽  
Citrullinated Proteins

BackgroundPeriodontitis (PD) is a known risk factor for rheumatoid arthritis (RA) and there is increasing evidence that the link between the two diseases is due to citrullination by the unique bacterial peptidylarginine deiminase (PAD) enzyme expressed by periodontal pathogenPophyromonas gingivalis(PPAD). However, the precise mechanism by which PPAD could generate potentially immunogenic peptides has remained controversial due to lack of information about the structural and catalytic mechanisms of the enzyme.ObjectivesBy solving the 3D structure of PPAD we aim to characterise activity and elucidate potential mechanisms involved in breach of tolerance to citrullinated proteins in RA.MethodsPPAD and a catalytically inactive mutant PPADC351Awere crystallised and their 3D structures solved. Key residues identified from 3D structures were examined by mutations. Fibrinogen and α-enolase were incubated with PPAD andP. gingivalisarginine gingipain (RgpB) and citrullinated peptides formed were sequenced and quantified by mass spectrometry.ResultsHere, we solve the crystal structure of a truncated, highly active form of PPAD. We confirm catalysis is mediated by the following residues: Asp130, His236, Asp238, Asn297 and Cys351 and show Arg152 and Arg154 may determine the substrate specificity of PPAD for C-terminal arginines. We demonstrate the formation of 37 C-terminally citrullinated peptides from fibrinogen and 11 from α-enolase following incubation with tPPAD and RgpB.ConclusionsPPAD displays an unequivocal specificity for C-terminal arginine residues and readily citrullinates peptides from key RA autoantigens. The formation of these novel citrullinated peptides may be involved in breach of tolerance to citrullinated proteins in RA.

The 1.9 Å Resolution Crystal Structure of Phosphono-CheY, an Analogue of the Active Form of the Response Regulator, CheY†,‡

Biochemistry ◽  
2000 ◽  
Vol 39 (18) ◽  
pp. 5280-5286 ◽  
Author(s):  
Christopher J. Halkides ◽  
Megan M. McEvoy ◽  
Eric Casper ◽  
Philip Matsumura ◽  
Karl Volz ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Response Regulator ◽  
Active Form
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