4G9I

Crystal structure of T.kodakarensis HypF

Summary for 4G9I

• Entry DOI: 10.2210/pdb4g9i/pdb
• Descriptor: Hydrogenase maturation protein HypF, ZINC ION (2 entities in total)
• Functional Keywords: zinc finger, hydrogenase maturation, atp binding, carbamoylation, transferase
• Biological source: Thermococcus kodakarensis
• Total number of polymer chains: 6
• Total formula weight: 527027.39

Authors

Tominaga, T.,Watanabe, S.,Matsumi, R.,Atomi, H.,Imanaka, T.,Miki, K. (deposition date: 2012-07-24, release date: 2012-10-24, Last modification date: 2024-11-13)

Primary citation

Tominaga, T.,Watanabe, S.,Matsumi, R.,Atomi, H.,Imanaka, T.,Miki, K.
Structure of the [NiFe]-hydrogenase maturation protein HypF from Thermococcus kodakarensis KOD1.
Acta Crystallogr.,Sect.F, 68:1153-1157, 2012

PubMed 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.

PubMed: 23027738
DOI: 10.1107/S1744309112036421

Experimental method

X-RAY DIFFRACTION (4.5 Å)