2z1t: Difference between revisions

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[[Image:2z1t.gif|left|200px]]
{{Seed}}
[[Image:2z1t.png|left|200px]]


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{{STRUCTURE_2z1t|  PDB=2z1t  |  SCENE=  }}  
{{STRUCTURE_2z1t|  PDB=2z1t  |  SCENE=  }}  


'''Crystal Structure of Hydrogenase Maturation Protein HypE'''
===Crystal Structure of Hydrogenase Maturation Protein HypE===




==Overview==
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The hydrogenase maturation protein HypE serves an essential function in the biosynthesis of the nitrile group, which is subsequently coordinated to Fe as CN(-) ligands in [Ni-Fe] hydrogenase. Here, we present the crystal structures of HypE from Desulfovibrio vulgaris Hildenborough in the presence and in the absence of ATP at a resolution of 2.0 A and 2.6 A, respectively. Comparison of the apo structure with the ATP-bound structure reveals that binding ATP causes an induced-fit movement of the N-terminal portion, but does not entail an overall structural change. The residue Cys341 at the C terminus, whose thiol group is supposed to be carbamoylated before the nitrile group synthesis, is completely buried within the protein and is located in the vicinity of the gamma-phosphate group of the bound ATP. This suggests that the catalytic reaction occurs in this configuration but that a conformational change is required for the carbamoylation of Cys341. A glutamate residue is found close to the thiol group as well, which is suggestive of deprotonation of the carbamoyl group at the beginning of the reactions.
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{{ABSTRACT_PUBMED_17706667}}


==About this Structure==
==About this Structure==
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[[Category: Beta barrel]]
[[Category: Beta barrel]]
[[Category: Lyase]]
[[Category: Lyase]]
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Revision as of 07:14, 28 July 2008

File:2z1t.png

Template:STRUCTURE 2z1t

Crystal Structure of Hydrogenase Maturation Protein HypE

Template:ABSTRACT PUBMED 17706667

About this Structure

2Z1T is a Single protein structure of sequence from Desulfovibrio vulgaris. Full crystallographic information is available from OCA.

Reference

Crystal structures of hydrogenase maturation protein HypE in the Apo and ATP-bound forms., Shomura Y, Komori H, Miyabe N, Tomiyama M, Shibata N, Higuchi Y, J Mol Biol. 2007 Sep 28;372(4):1045-54. Epub 2007 Jul 26. PMID:17706667

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