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| | <StructureSection load='2rb9' size='340' side='right'caption='[[2rb9]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='2rb9' size='340' side='right'caption='[[2rb9]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2rb9]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Eco57 Eco57]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RB9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RB9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2rb9]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RB9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RB9 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2i6r|2i6r]]</div></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]] 2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hypE, ECs3586 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 ECO57])</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=2rb9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rb9 OCA], [https://pdbe.org/2rb9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rb9 RCSB], [https://www.ebi.ac.uk/pdbsum/2rb9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rb9 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=2rb9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rb9 OCA], [https://pdbe.org/2rb9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rb9 RCSB], [https://www.ebi.ac.uk/pdbsum/2rb9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rb9 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A0H3JHA1_ECO57 A0A0H3JHA1_ECO57] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Eco57]] | + | [[Category: Escherichia coli O157:H7]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Asinas, A E]] | + | [[Category: Asinas AE]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Cygler M]] |
| - | [[Category: Cygler, M]] | + | [[Category: Matte A]] |
| - | [[Category: Matte, A]] | + | [[Category: Min T]] |
| - | [[Category: Min, T]] | + | [[Category: Munger C]] |
| - | [[Category: Munger, C]] | + | [[Category: Proteau A]] |
| - | [[Category: Proteau, A]] | + | [[Category: Rangarajan ES]] |
| - | [[Category: Rangarajan, E S]] | + | |
| - | [[Category: Bsgi]]
| + | |
| - | [[Category: Dimer]]
| + | |
| - | [[Category: Enzyme]]
| + | |
| - | [[Category: Hydrogenase maturation]]
| + | |
| - | [[Category: Unknown function]]
| + | |
| Structural highlights
Function
A0A0H3JHA1_ECO57
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
Hydrogenases are enzymes involved in hydrogen metabolism, utilizing H2 as an electron source. [NiFe] hydrogenases are heterodimeric Fe-S proteins, with a large subunit containing the reaction center involving Fe and Ni metal ions and a small subunit containing one or more Fe-S clusters. Maturation of the [NiFe] hydrogenase involves assembly of nonproteinaceous ligands on the large subunit by accessory proteins encoded by the hyp operon. HypE is an essential accessory protein and participates in the synthesis of two cyano groups found in the large subunit. We report the crystal structure of Escherichia coli HypE at 2.0-A resolution. HypE exhibits a fold similar to that of PurM and ThiL and forms dimers. The C-terminal catalytically essential Cys336 is internalized at the dimer interface between the N- and C-terminal domains. A mechanism for dehydration of the thiocarbamate to the thiocyanate is proposed, involving Asp83 and Glu272. The interactions of HypE and HypF were characterized in detail by surface plasmon resonance and isothermal titration calorimetry, revealing a Kd (dissociation constant) of approximately 400 nM. The stoichiometry and molecular weights of the complex were verified by size exclusion chromatography and gel scanning densitometry. These experiments reveal that HypE and HypF associate to form a stoichiometric, hetero-oligomeric complex predominantly consisting of a [EF]2 heterotetramer which exists in a dynamic equilibrium with the EF heterodimer. The surface plasmon resonance results indicate that a conformational change occurs upon heterodimerization which facilitates formation of a productive complex as part of the carbamate transfer reaction.
Structure of [NiFe] hydrogenase maturation protein HypE from Escherichia coli and its interaction with HypF.,Rangarajan ES, Asinas A, Proteau A, Munger C, Baardsnes J, Iannuzzi P, Matte A, Cygler M J Bacteriol. 2008 Feb;190(4):1447-58. Epub 2007 Dec 7. PMID:18065529[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Rangarajan ES, Asinas A, Proteau A, Munger C, Baardsnes J, Iannuzzi P, Matte A, Cygler M. Structure of [NiFe] hydrogenase maturation protein HypE from Escherichia coli and its interaction with HypF. J Bacteriol. 2008 Feb;190(4):1447-58. Epub 2007 Dec 7. PMID:18065529 doi:http://dx.doi.org/10.1128/JB.01610-07
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