ArticleActa crystallographica. Section F, Structural biology and crystallization communications2012
Structure of the [NiFe]-hydrogenase maturation protein HypF from Thermococcus kodakarensis KOD1.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 12 citations in OpenAlex.
- An overview of 25 years of research on Thermococcus kodakarensis, a genetically versatile model organism for archaeal research.Folia microbiologica · 2020Review
- Anaerobic Formate and Hydrogen Metabolism.EcoSal Plus · 2016Review
- Can I solve my structure by SAD phasing? Planning an experiment, scaling data and evaluating the useful anomalous correlation and anomalous signal.Acta crystallographica. Section D, Structural biology · 2016Article
- Can I solve my structure by SAD phasing? Anomalous signal in SAD phasing.Acta crystallographica. Section D, Structural biology · 2016Article
- Article
- The influence of oxygen on [NiFe]-hydrogenase cofactor biosynthesis and how ligation of carbon monoxide precedes cyanation.PloS one · 2014Article
- Crystal structures of the carbamoylated and cyanated forms of HypE for [NiFe] hydrogenase maturation.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
HypF is involved in the biosynthesis of the CN ligand of the NiFe(CN)(2)CO centre of [NiFe]-hydrogenases. Here, the full-length structure of HypF from Thermococcus kodakarenesis is reported at 4.5 Å resolution. The N-terminal acylphosphatase-like (ACP) domain interacts with the zinc-finger domain with some flexibility in its relative position. Molecular-surface analysis shows that a deep pocket formed between the ACP and zinc-finger domains is highly conserved and has positive potential. These results suggest that the positively charged pocket identified is involved in the hydrolysis of carbamoyl phosphate and the formation of a carbamoyl intermediate.
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