2hf9: Difference between revisions
New page: left|200px<br /><applet load="2hf9" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hf9, resolution 1.900Å" /> '''Crystal structure o... |
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[[Image:2hf9.gif|left|200px]]<br /><applet load="2hf9" size=" | [[Image:2hf9.gif|left|200px]]<br /><applet load="2hf9" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2hf9, resolution 1.900Å" /> | caption="2hf9, resolution 1.900Å" /> | ||
'''Crystal structure of HypB from Methanocaldococcus jannaschii in the triphosphate form'''<br /> | '''Crystal structure of HypB from Methanocaldococcus jannaschii in the triphosphate form'''<br /> | ||
==Overview== | ==Overview== | ||
HypB is a prokaryotic metal-binding guanine nucleotide-binding protein | 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== | ==About this Structure== | ||
2HF9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii] with MG, ZN and GSP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 2HF9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=GSP:'>GSP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HF9 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: p-loop containing nucleoside triphosphate hydrolase]] | [[Category: p-loop containing nucleoside triphosphate hydrolase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:41:13 2008'' | ||
Revision as of 15:41, 21 February 2008
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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 with MG, ZN and GSP as ligands. 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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