2hf9
From Proteopedia
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|PDB= 2hf9 |SIZE=350|CAPTION= <scene name='initialview01'>2hf9</scene>, resolution 1.900Å | |PDB= 2hf9 |SIZE=350|CAPTION= <scene name='initialview01'>2hf9</scene>, resolution 1.900Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=GSP:5 | + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=GSP:5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE'>GSP</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= hypB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 Methanocaldococcus jannaschii]) | |GENE= hypB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 Methanocaldococcus jannaschii]) | ||
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[[Category: p-loop containing nucleoside triphosphate hydrolase]] | [[Category: p-loop containing nucleoside triphosphate hydrolase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 15:15:13 2008'' |
Revision as of 13:15, 23 March 2008
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| , resolution 1.900Å | |||||||
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| Ligands: | , and | ||||||
| Gene: | hypB (Methanocaldococcus jannaschii) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of HypB from Methanocaldococcus jannaschii in the triphosphate form
Overview
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 Structure
2HF9 is a Single protein structure of sequence from Methanocaldococcus jannaschii. Full crystallographic information is available from OCA.
Reference
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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