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| | ==Solution structure of oxidized bovine microsomal cytochrome B5 Mutant V45H== | | ==Solution structure of oxidized bovine microsomal cytochrome B5 Mutant V45H== |
| - | <StructureSection load='1sh4' size='340' side='right'caption='[[1sh4]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''> | + | <StructureSection load='1sh4' size='340' side='right'caption='[[1sh4]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1sh4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SH4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SH4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1sh4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SH4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SH4 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1nx7|1nx7]]</td></tr> | + | <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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1sh4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sh4 OCA], [http://pdbe.org/1sh4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1sh4 RCSB], [http://www.ebi.ac.uk/pdbsum/1sh4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1sh4 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=1sh4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sh4 OCA], [https://pdbe.org/1sh4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sh4 RCSB], [https://www.ebi.ac.uk/pdbsum/1sh4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sh4 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CYB5_BOVIN CYB5_BOVIN]] Cytochrome b5 is a membrane bound hemoprotein which function as an electron carrier for several membrane bound oxygenases. | + | [https://www.uniprot.org/uniprot/CYB5_BOVIN CYB5_BOVIN] 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: Bovin]] | + | [[Category: Bos taurus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Wu, H]] | + | [[Category: Wu H]] |
| - | [[Category: Zhang, Q]] | + | [[Category: Zhang Q]] |
| - | [[Category: Electron transport]]
| + | |
| - | [[Category: Five helix]]
| + | |
| - | [[Category: Five sheet]]
| + | |
| - | [[Category: Heme ring]]
| + | |
| Structural highlights
Function
CYB5_BOVIN 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 PubMed
A comparative study on the solution structures of bovine microsomal cytochrome b5 (Tb5) and the mutant V45H has been achieved by 1D and 2D 1H-NMR spectroscopy to clarify the differences in the solution conformations between these two proteins. The results reveal that the global folding of the V45H mutant in solution is unchanged, but the subtle changes exist in the orientation of the axial ligand His39, and heme vinyl groups. The side chain of His45 in V45H mutant extends to the outer edge of the heme pocket leaving a cavity at the site originally occupied by the inner methyl group of Val45 residue. In addition, the imidazole ring of axial ligand His39 rotates counterclockwise by approximately 3 degrees around the His-Fe-His axis, and the 4-heme vinyl group turns to the space vacated by the removed side chain due to the mutation. Furthermore, the helix III of the heme pocket undergoes outward displacement, while the linkage between helix II and III is shifted leftward. These observations are not only consistent with the pattern of the pseudocontact shifts of the heme protons, but also well account for the lower stability of V45H mutant against heat and urea.
The comparative study on the solution structures of the oxidized bovine microsomal cytochrome b5 and mutant V45H.,Zhang Q, Cao C, Wang ZQ, Wang YH, Wu H, Huang ZX Protein Sci. 2004 Aug;13(8):2161-9. PMID:15273310[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Zhang Q, Cao C, Wang ZQ, Wang YH, Wu H, Huang ZX. The comparative study on the solution structures of the oxidized bovine microsomal cytochrome b5 and mutant V45H. Protein Sci. 2004 Aug;13(8):2161-9. PMID:15273310 doi:10.1110/ps.04721104
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