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3a43

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Revision as of 14:26, 22 December 2016

Crystal structure of HypA

Structural highlights

3a43 is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Related:	3a44
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3a43"

@@ Line 1: / Line 1: @@
-==Crystal sructure of HypA==
+==Crystal structure of HypA==
 <StructureSection load='3a43' size='340' side='right' caption='[[3a43]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3a43]] is a 2 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=3A43 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3A43 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3a43]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3A43 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>
 <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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3a44|3a44]]</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>
+<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=3a43 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a43 OCA], [http://pdbe.org/3a43 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3a43 RCSB], [http://www.ebi.ac.uk/pdbsum/3a43 PDBsum], [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3a43 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a43 OCA], [http://pdbe.org/3a43 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3a43 RCSB], [http://www.ebi.ac.uk/pdbsum/3a43 PDBsum]</span></td></tr>
 </table>
 == Function ==

3a43

From Proteopedia

Revision as of 14:26, 22 December 2016

Crystal structure of HypA

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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