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| | ==Crystal structure of HypA in the dimeric form== | | ==Crystal structure of HypA in the dimeric form== |
| - | <StructureSection load='3a44' size='340' side='right' caption='[[3a44]], [[Resolution|resolution]] 3.31Å' scene=''> | + | <StructureSection load='3a44' size='340' side='right'caption='[[3a44]], [[Resolution|resolution]] 3.31Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3a44]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_kodakaraensis_(strain_kod1) Pyrococcus kodakaraensis (strain kod1)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A44 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3A44 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3a44]] is a 4 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=3A44 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A44 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.31Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene></td></tr> | + | <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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3a43|3a43]]</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=3a44 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a44 OCA], [https://pdbe.org/3a44 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a44 RCSB], [https://www.ebi.ac.uk/pdbsum/3a44 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a44 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hypA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=69014 Pyrococcus kodakaraensis (strain KOD1)])</td></tr>
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| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3a44 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a44 OCA], [http://pdbe.org/3a44 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3a44 RCSB], [http://www.ebi.ac.uk/pdbsum/3a44 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3a44 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/HYPA_THEKO HYPA_THEKO]] Probably plays a role in a hydrogenase nickel cofactor insertion step (By similarity). | + | [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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| | ==See Also== | | ==See Also== |
| - | *[[HypA-HypB-HypC-HypD-HypE-HypF|HypA-HypB-HypC-HypD-HypE-HypF]] | + | *[[HypA%2C HypB%2C HypC%2C HypD%2C HypE and HypF 3D structures|HypA%2C HypB%2C HypC%2C HypD%2C HypE and HypF 3D structures]] |
| - | *[[Molecular Playground/HypA|Molecular Playground/HypA]]
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| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Arai, T]] | + | [[Category: Large Structures]] |
| - | [[Category: Atomi, H]] | + | [[Category: Thermococcus kodakarensis KOD1]] |
| - | [[Category: Imanaka, T]] | + | [[Category: Arai T]] |
| - | [[Category: Matsumi, R]] | + | [[Category: Atomi H]] |
| - | [[Category: Miki, K]] | + | [[Category: Imanaka T]] |
| - | [[Category: Watanabe, S]] | + | [[Category: Matsumi R]] |
| - | [[Category: Domain swapping]] | + | [[Category: Miki K]] |
| - | [[Category: Metal binding protein]] | + | [[Category: Watanabe S]] |
| - | [[Category: Metal-binding]]
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| - | [[Category: Nickel]]
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| - | [[Category: Nickel binding]]
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| - | [[Category: Zinc-finger]]
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| Structural highlights
Function
HYPA_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 PubMed
HypA 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 Also
References
- ↑ Watanabe S, Arai T, Matsumi R, Atomi H, Imanaka T, Miki K. Crystal structure of HypA, a nickel-binding metallochaperone for [NiFe] hydrogenase maturation. J Mol Biol. 2009 Dec 4;394(3):448-59. Epub 2009 Sep 19. PMID:19769985 doi:10.1016/j.jmb.2009.09.030
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