2011
DOI: 10.1074/jbc.m111.281956
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Crystal Structure of HydF Scaffold Protein Provides Insights into [FeFe]-Hydrogenase Maturation

Abstract: Background: HydF is a GTPase essential for maturation of [FeFe]-hydrogenase. Results: The first crystal structure of HydF has been determined. Conclusion:The protein monomer comprises a GTP-binding domain, a dimerization domain, and a metal-cluster binding domain. Two monomers dimerize, and two dimers can aggregate to a tetramer. Significance: The crystal structure of the latter furnishes several clues about the events necessary for cluster generation.

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Cited by 34 publications
(71 citation statements)
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“…Based on this analysis, we found a stoichiometric ratio of roughly 1:4 for the HydE-6His⅐HydF-StrepII complex and of 1:1 for the HydG6His⅐HydF-StrepII complex. The observed stoichiometries could be due to the presence of multiple oligomeric species of HydFStrepII protein (dimers and tetramers) (22), as well as to the amount of HydE-6His, which is invariably lower when compared with HydG-6His in co-expression experiments (not shown).…”
Section: Biochemical Analysis Of Protein-protein Interactions Of Hydfmentioning
confidence: 99%
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“…Based on this analysis, we found a stoichiometric ratio of roughly 1:4 for the HydE-6His⅐HydF-StrepII complex and of 1:1 for the HydG6His⅐HydF-StrepII complex. The observed stoichiometries could be due to the presence of multiple oligomeric species of HydFStrepII protein (dimers and tetramers) (22), as well as to the amount of HydE-6His, which is invariably lower when compared with HydG-6His in co-expression experiments (not shown).…”
Section: Biochemical Analysis Of Protein-protein Interactions Of Hydfmentioning
confidence: 99%
“…As reported in the Introduction, we recently solved the three-dimensional crystal structure of a nucleotide-free HydF protein (22) and showed that the GTP-binding domain includes a flexible loop that is expected to undergo a structural rearrangement upon nucleotide binding and/or hydrolysis that could in turn influence the interaction of the scaffold with the maturation partners. This prompted us to further investigate the role of this domain in the functional and structural network of the [FeFe]-hydrogenase maturation proteins.…”
Section: Investigating the Potential Involvement Of Gtp Binding/hydromentioning
confidence: 99%
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“…Both HydE and HydG are members of the large radical S-adenosyl-L-methionine (SAM) protein family (16,17). With the recent reports of HydG crystal structures from Carboxydothermus hydrogenoformans (Ch) by us (18) and from Thermoanaerobacter italicus (Ti) by Dinis et al (19), X-ray models are now available for the three maturases (20,21); however, unambiguous structure-function relationships have been proposed only in the case of HydG. Indeed, site-directed mutational studies have shown that CO and CN − syntheses are affected by either the deletion of the maturase C-terminal region, where a second iron-sulfur cluster binds (22), or Cys-to-Ser mutations in its corresponding CxxCx 22 C binding motif (10,13).…”
mentioning
confidence: 99%