Crystal structures of hydrogenase maturation protein HypE in the Apo and ATP-bound forms |
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Authors: | Shomura Yasuhito Komori Hirofumi Miyabe Natsuko Tomiyama Masamitsu Shibata Naoki Higuchi Yoshiki |
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Affiliation: | Department of Life Science, Graduate School of Life Science, University of Hyogo, 3-2-1 Koto, Ako-Gun, Hyogo, Japan. shomura@sci.u-hyogo.ac.jp |
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Abstract: | 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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Keywords: | [NiFe] hydrogenase X-ray crystallography carbamoyl group ATP-binding PurM family |
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