کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2187982 | 1096148 | 2007 | 10 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Crystal Structures of Hydrogenase Maturation Protein HypE in the Apo and ATP-bound Forms Crystal Structures of Hydrogenase Maturation Protein HypE in the Apo and ATP-bound Forms](/preview/png/2187982.png)
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 Å and 2.6 Å, 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 γ-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.
Journal: Journal of Molecular Biology - Volume 372, Issue 4, 28 September 2007, Pages 1045–1054