2hf9

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[[Image:2hf9.gif|left|200px]]
[[Image:2hf9.gif|left|200px]]
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{{Structure
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|PDB= 2hf9 |SIZE=350|CAPTION= <scene name='initialview01'>2hf9</scene>, resolution 1.900&Aring;
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The line below this paragraph, containing "STRUCTURE_2hf9", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=GSP:5&#39;-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE'>GSP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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|GENE= hypB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 Methanocaldococcus jannaschii])
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|DOMAIN=
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{{STRUCTURE_2hf9| PDB=2hf9 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hf9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hf9 OCA], [http://www.ebi.ac.uk/pdbsum/2hf9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2hf9 RCSB]</span>
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'''Crystal structure of HypB from Methanocaldococcus jannaschii in the triphosphate form'''
'''Crystal structure of HypB from Methanocaldococcus jannaschii in the triphosphate form'''
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[[Category: Scrima, A.]]
[[Category: Scrima, A.]]
[[Category: Wittinghofer, A.]]
[[Category: Wittinghofer, A.]]
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[[Category: alpha and beta protein]]
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[[Category: Alpha and beta protein]]
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[[Category: p-loop containing nucleoside triphosphate hydrolase]]
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[[Category: P-loop containing nucleoside triphosphate hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:13:24 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:29:33 2008''
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Revision as of 03:13, 4 May 2008

Template:STRUCTURE 2hf9

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 Page seeded by OCA on Sun May 4 06:13:24 2008

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