2i6r: Difference between revisions

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OCA

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 <StructureSection load='2i6r' size='340' side='right'caption='[[2i6r]], [[Resolution|resolution]] 2.51&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2i6r]] 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=2I6R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2I6R FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2i6r]] 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=2I6R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2I6R FirstGlance]. <br>
-</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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.51&#8491;</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=2i6r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i6r OCA], [https://pdbe.org/2i6r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2i6r RCSB], [https://www.ebi.ac.uk/pdbsum/2i6r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2i6r ProSAT], [https://www.topsan.org/Proteins/BSGI/2i6r TOPSAN]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/HYPE_ECOLI HYPE_ECOLI] Involved in the maturation of [NiFe] hydrogenases. Along with HypF, it catalyzes the synthesis of the CN ligands of the active site iron of [NiFe]-hydrogenases. HypE catalyzes the ATP-dependent dehydration of the carboxamido group attached to its C-terminal cysteine to a cyano group (PubMed:12586941, PubMed:15291820). The cyano group is then transferred from HypE to the HypC-HypD complex or the HybG-HypD complex (PubMed:15504408).<ref>PMID:12586941</ref> <ref>PMID:15291820</ref> <ref>PMID:15504408</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 17: / Line 19: @@
 </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=2i6r ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== 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<ref>PMID:18065529</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 2i6r" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 33: / Line 26: @@
 __TOC__
 </StructureSection>
-[[Category: Eco57]]
+[[Category: Escherichia coli O157:H7]]
 [[Category: Large Structures]]
-[[Category: Structural genomic]]
+[[Category: Cygler M]]
-[[Category: Cygler, M]]
+[[Category: Iannuzzi P]]
-[[Category: Iannuzzi, P]]
+[[Category: Matte A]]
-[[Category: Matte, A]]
+[[Category: Proteau A]]
-[[Category: Proteau, A]]
+[[Category: Rangarajan ES]]
-[[Category: Rangarajan, E S]]
-[[Category: Bsgi]]
-[[Category: Hydrogenase maturation protein]]
-[[Category: Hype]]
-[[Category: Unknown function]]