2hf8: Difference between revisions

Revision as of 18:41, 21 February 2008

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 with , and as ligands. 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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-[[Image:2hf8.gif|left|200px]]<br /><applet load="2hf8" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2hf8.gif|left|200px]]<br /><applet load="2hf8" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2hf8, resolution 2.100&Aring;" />
 '''Crystal structure of HypB from Methanocaldococcus jannaschii in the triphosphate form, in complex with zinc'''<br />
 ==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.
+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==
-HF8 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2HF8 OCA].
+HF8 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=2HF8 OCA].
 ==Reference==
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 [[Category: p-loop containing nucleoside triphosphate hydrolase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 11:42:48 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:41:15 2008''