2hf8
| |||||||
| , resolution 2.100Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , and | ||||||
| Gene: | hypB (Methanocaldococcus jannaschii) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of HypB from Methanocaldococcus jannaschii in the triphosphate form, in complex with zinc
OverviewOverview
HypB is a prokaryotic metal-binding guanine nucleotide-binding protein that is essential for nickel incorporation into hydrogenases. Here we solved the x-ray structure of HypB from Methanocaldococcus jannaschii. It shows that the G-domain has a different topology than the Ras-like proteins and belongs to the SIMIBI (after Signal Recognition Particle, MinD and BioD) class of NTP-binding proteins. We show that HypB undergoes nucleotide-dependent dimerization, which is apparently a common feature of SIMIBI class G-proteins. The nucleotides are located in the dimer interface and are contacted by both subunits. The active site features residues from both subunits arguing that hydrolysis also requires dimerization. Two metal-binding sites are found, one of which is dependent on the state of bound nucleotide. A totally conserved ENV/IGNLV/ICP motif in switch II relays the nucleotide binding with the metal ionbinding site. The homology with NifH, the Fe protein subunit of nitrogenase, suggests a mechanistic model for the switch-dependent incorporation of a metal ion into hydrogenases.
About this StructureAbout this Structure
2HF8 is a Single protein structure of sequence from Methanocaldococcus jannaschii. Full crystallographic information is available from OCA.
ReferenceReference
Structural insights into HypB, a GTP-binding protein that regulates metal binding., Gasper R, Scrima A, Wittinghofer A, J Biol Chem. 2006 Sep 15;281(37):27492-502. Epub 2006 Jun 28. PMID:16807243
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