2z1t
From Proteopedia
(Difference between revisions)
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<StructureSection load='2z1t' size='340' side='right'caption='[[2z1t]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='2z1t' size='340' side='right'caption='[[2z1t]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2z1t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2z1t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Desulfovibrio_vulgaris_str._Hildenborough Desulfovibrio vulgaris str. Hildenborough]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z1T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Z1T 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]] 2.6Å</td></tr> |
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2z1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z1t OCA], [https://pdbe.org/2z1t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2z1t RCSB], [https://www.ebi.ac.uk/pdbsum/2z1t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2z1t 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=2z1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z1t OCA], [https://pdbe.org/2z1t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2z1t RCSB], [https://www.ebi.ac.uk/pdbsum/2z1t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2z1t ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q72F88_DESVH Q72F88_DESVH] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2z1t ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2z1t ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The hydrogenase maturation protein HypE serves an essential function in the biosynthesis of the nitrile group, which is subsequently coordinated to Fe as CN(-) ligands in [Ni-Fe] hydrogenase. Here, we present the crystal structures of HypE from Desulfovibrio vulgaris Hildenborough in the presence and in the absence of ATP at a resolution of 2.0 A and 2.6 A, respectively. Comparison of the apo structure with the ATP-bound structure reveals that binding ATP causes an induced-fit movement of the N-terminal portion, but does not entail an overall structural change. The residue Cys341 at the C terminus, whose thiol group is supposed to be carbamoylated before the nitrile group synthesis, is completely buried within the protein and is located in the vicinity of the gamma-phosphate group of the bound ATP. This suggests that the catalytic reaction occurs in this configuration but that a conformational change is required for the carbamoylation of Cys341. A glutamate residue is found close to the thiol group as well, which is suggestive of deprotonation of the carbamoyl group at the beginning of the reactions. | ||
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| - | Crystal structures of hydrogenase maturation protein HypE in the Apo and ATP-bound forms.,Shomura Y, Komori H, Miyabe N, Tomiyama M, Shibata N, Higuchi Y J Mol Biol. 2007 Sep 28;372(4):1045-54. Epub 2007 Jul 26. PMID:17706667<ref>PMID:17706667</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2z1t" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[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]] | *[[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]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Desulfovibrio vulgaris str. Hildenborough]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Higuchi | + | [[Category: Higuchi Y]] |
| - | [[Category: Shomura | + | [[Category: Shomura Y]] |
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Current revision
Crystal Structure of Hydrogenase Maturation Protein HypE
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