2z1t
From Proteopedia
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Crystal Structure of Hydrogenase Maturation Protein HypE
Overview
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.
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
Page seeded by OCA on Wed Jan 23 13:05:28 2008
