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| {{STRUCTURE_2z1u| PDB=2z1u | SCENE= }} | | {{STRUCTURE_2z1u| PDB=2z1u | SCENE= }} |
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| '''Crystal Structure of Hydrogenase Maturation Protein HypE in complex with ATP'''
| | ===Crystal Structure of Hydrogenase Maturation Protein HypE in complex with ATP=== |
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| ==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. | | The line below this paragraph, {{ABSTRACT_PUBMED_17706667}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17706667 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17706667}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Beta barrel]] | | [[Category: Beta barrel]] |
| [[Category: Lyase]] | | [[Category: Lyase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 19:50:22 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:45:19 2008'' |
