3a43: Difference between revisions
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<StructureSection load='3a43' size='340' side='right'caption='[[3a43]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='3a43' size='340' side='right'caption='[[3a43]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3a43]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3a43]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermococcus_kodakarensis_KOD1 Thermococcus kodakarensis KOD1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A43 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A43 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3a43 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a43 OCA], [https://pdbe.org/3a43 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a43 RCSB], [https://www.ebi.ac.uk/pdbsum/3a43 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a43 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3a43 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a43 OCA], [https://pdbe.org/3a43 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a43 RCSB], [https://www.ebi.ac.uk/pdbsum/3a43 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a43 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/HYPA_THEKO HYPA_THEKO] Probably plays a role in a hydrogenase nickel cofactor insertion step (By similarity). | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a4/3a43_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a4/3a43_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Arai | [[Category: Thermococcus kodakarensis KOD1]] | ||
[[Category: Aromi | [[Category: Arai T]] | ||
[[Category: Imanaka | [[Category: Aromi H]] | ||
[[Category: Matsumi | [[Category: Imanaka T]] | ||
[[Category: Miki | [[Category: Matsumi R]] | ||
[[Category: Watanabe | [[Category: Miki K]] | ||
[[Category: Watanabe S]] | |||
Latest revision as of 08:39, 17 October 2024
Crystal structure of HypACrystal structure of HypA
Structural highlights
FunctionHYPA_THEKO Probably plays a role in a hydrogenase nickel cofactor insertion step (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedHypA is one of the auxiliary proteins involved in the maturation of [NiFe] hydrogenases. By an unknown mechanism, HypA functions as a metallochaperone in the insertion of the Ni atom into hydrogenases. We have determined the crystal structures of HypA from Thermococcus kodakaraensis KOD1 in both monomeric and dimeric states. The structure of the HypA monomer consists of Ni- and Zn-binding domains. The relative arrangement of the two metal-binding domains has been shown to be associated with local conformations of the conserved Ni-binding motif, suggesting a communication between the Ni- and Zn-binding sites. The HypA dimer has been shown to be stabilized by unexpected domain swapping through archaea-specific linker helices. In addition, the hexameric structure of HypA is formed in the crystal packing. Several hydrogen bonds and hydrophobic interactions stabilize the hexamer interface. These findings suggest the functional diversity of HypA proteins. Crystal structure of HypA, a nickel-binding metallochaperone for [NiFe] hydrogenase maturation.,Watanabe S, Arai T, Matsumi R, Atomi H, Imanaka T, Miki K J Mol Biol. 2009 Dec 4;394(3):448-59. Epub 2009 Sep 19. PMID:19769985[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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