1eue: Difference between revisions
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<StructureSection load='1eue' size='340' side='right'caption='[[1eue]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='1eue' size='340' side='right'caption='[[1eue]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1eue]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1eue]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EUE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EUE 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]] 1.8Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></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=1eue FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eue OCA], [https://pdbe.org/1eue PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eue RCSB], [https://www.ebi.ac.uk/pdbsum/1eue PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eue 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=1eue FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eue OCA], [https://pdbe.org/1eue PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eue RCSB], [https://www.ebi.ac.uk/pdbsum/1eue PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eue ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/CYB5B_RAT CYB5B_RAT] Cytochrome b5 is a membrane bound hemoprotein which function as an electron carrier for several membrane bound oxygenases. | |||
== 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: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Rattus norvegicus]] | ||
[[Category: | [[Category: Oganesyan V]] | ||
[[Category: | [[Category: Zhang X]] | ||
Latest revision as of 09:00, 9 August 2023
RAT OUTER MITOCHONDRIAL MEMBRANE CYTOCHROME B5RAT OUTER MITOCHONDRIAL MEMBRANE CYTOCHROME B5
Structural highlights
FunctionCYB5B_RAT Cytochrome b5 is a membrane bound hemoprotein which function as an electron carrier for several membrane bound oxygenases. 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 PubMedThe reduction potential of cytochrome b5 is modulated via the formation of a complex with polylysine at the electrode surface (Rivera et al., Biochemistry, 1998, 37, 1485). This modulation is thought to originate from the neutralization of a solvent exposed heme propionate and from dehydration of the complex interface. Although direct evidence demonstrating that neutralization of the charge on the heme propionate contributes to the modulation of the redox potential of cytochrome b5 has been obtained, evidence demonstrating that water exclusion from the complex interface plays a similar role has not been conclusive. Herein we report the preparation of the V45I/V61I double mutant of rat liver outer mitochondrial membrane (OM) cytochrome b5. This mutant has been engineered with the aim of restricting water accessibility to the exposed heme edge of cytochrome b5. The X-ray crystal structure of the V45I/V61I mutant revealed that the side chain of Ile at positions 45 and 61 restricts water accessibility to the interior of the heme cavity and protects a large section of the heme edge from the aqueous environment. Electrochemical studies performed with the V45I/V61I mutant of cytochrome b5, and with a derivative in which the heme propionates have been converted into the corresponding dimethyl ester groups, clearly demonstrate that dehydration of the heme edge contributes to the modulation of the reduction potential of cytochrome b5. In fact, these studies showed that exclusion of water from the complex interface exerts an effect (approximately 40 mV shift) that is comparable, if not larger, than the one originating from neutralization of the charge on the solvent exposed heme propionate (approximately 30 mV shift). Modulation of redox potential in electron transfer proteins: effects of complex formation on the active site microenvironment of cytochrome b5.,Wirtz M, Oganesyan V, Zhang X, Studer J, Rivera M Faraday Discuss. 2000;(116):221-34; discussion 257-68. PMID:11197480[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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