1lr6: Difference between revisions
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< | ==Crystal structure of V45Y mutant of cytochrome b5== | ||
<StructureSection load='1lr6' size='340' side='right'caption='[[1lr6]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1lr6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LR6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LR6 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</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'>[https://proteopedia.org/fgij/fg.htm?mol=1lr6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lr6 OCA], [https://pdbe.org/1lr6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lr6 RCSB], [https://www.ebi.ac.uk/pdbsum/1lr6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lr6 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[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 == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lr/1lr6_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=1lr6 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Val45 is a highly conserved residue and a component of the heme-pocket wall of cytochrome b(5). The crystal structures of cytochrome b(5) mutants V45E and V45Y have been determined at high resolution. Their overall structures were very similar to that of the wild-type protein. However, Val45 of the wild-type protein points towards the heme, but the large side chains of both Glu45 and Tyr45 of the mutants point towards the solvent. A channel is thus opened and the hydrophobicity of the heme pocket is decreased. The rotation of the porphyrin ring and the conformational change of the axial ligand His39 in the V45Y mutant indicate that the microenvironment of the heme is disturbed because of the mutation. The binding constants and the electron-transfer rates between cytochrome b(5) and cytochrome c decrease owing to the mutation, which can be accounted for by molecular modeling: the inter-iron distances increase in order to eliminate the unreasonably close contacts resulting from the large volumes of the mutated side chains. The influence of the mutations on the redox potentials and protein stability is also discussed. The structures of seven mutants of cytochrome b(5) are compared with each other and the effects of these mutations on the protein properties and functions are summarized. | |||
Structures of V45E and V45Y mutants and structure comparison of a variety of cytochrome b5 mutants.,Gan JH, Wu J, Wang ZQ, Wang YH, Huang ZX, Xia ZX Acta Crystallogr D Biol Crystallogr. 2002 Aug;58(Pt 8):1298-306. Epub 2002, Jul 20. PMID:12136141<ref>PMID:12136141</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1lr6" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Cytochrome b5 3D structures|Cytochrome b5 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
== | |||
< | |||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Gan | [[Category: Large Structures]] | ||
[[Category: Huang | [[Category: Gan J-H]] | ||
[[Category: Wang | [[Category: Huang Z-X]] | ||
[[Category: Wang | [[Category: Wang Y-H]] | ||
[[Category: Wu | [[Category: Wang Z-Q]] | ||
[[Category: Xia | [[Category: Wu J]] | ||
[[Category: Xia Z-X]] | |||
Latest revision as of 10:17, 25 October 2023
Crystal structure of V45Y mutant of cytochrome b5Crystal structure of V45Y mutant of cytochrome b5
Structural highlights
FunctionCYB5_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 PubMedVal45 is a highly conserved residue and a component of the heme-pocket wall of cytochrome b(5). The crystal structures of cytochrome b(5) mutants V45E and V45Y have been determined at high resolution. Their overall structures were very similar to that of the wild-type protein. However, Val45 of the wild-type protein points towards the heme, but the large side chains of both Glu45 and Tyr45 of the mutants point towards the solvent. A channel is thus opened and the hydrophobicity of the heme pocket is decreased. The rotation of the porphyrin ring and the conformational change of the axial ligand His39 in the V45Y mutant indicate that the microenvironment of the heme is disturbed because of the mutation. The binding constants and the electron-transfer rates between cytochrome b(5) and cytochrome c decrease owing to the mutation, which can be accounted for by molecular modeling: the inter-iron distances increase in order to eliminate the unreasonably close contacts resulting from the large volumes of the mutated side chains. The influence of the mutations on the redox potentials and protein stability is also discussed. The structures of seven mutants of cytochrome b(5) are compared with each other and the effects of these mutations on the protein properties and functions are summarized. Structures of V45E and V45Y mutants and structure comparison of a variety of cytochrome b5 mutants.,Gan JH, Wu J, Wang ZQ, Wang YH, Huang ZX, Xia ZX Acta Crystallogr D Biol Crystallogr. 2002 Aug;58(Pt 8):1298-306. Epub 2002, Jul 20. PMID:12136141[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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