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1awp

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RAT OUTER MITOCHONDRIAL MEMBRANE CYTOCHROME B5

Structural highlights

1awp is a 2 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CYB5B_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 PubMed

When the reduction potential of cytochrome b5 is measured with the aid of several different surface-modified electrodes that function on the basis of electrostatic interactions with the protein, the resultant values have been consistently more positive (40-100 mV) than the reduction potentials measured with potentiometric methods. In this paper, we report that the heme edge containing the exposed heme propionate, a heme methyl, and a heme vinyl, and which constitutes part of the surface of cytochrome b5, modulates its reduction potential. The positive shifts observed in the voltammetric measurements appear to originate from the formation of a complex between cytochrome b5 and the modified electrode surface which (a) neutralizes the charge on the heme propionate located on the exposed heme edge and (b) lowers the dielectric of the exposed heme microenvironment by excluding water from the complex interface, factors which result in the destabilization of the positive charge on the ferric heme with respect to the neutral ferrous heme. The observed positive shift, which is induced by complexation at the electrode surface, may indicate that similar shifts in the reduction potential of cytochrome b5 occur when it forms a complex with physiological partners, prior to electron transfer. The effect of the value of the dielectric constant on the reduction potential of cytochrome b5 was corroborated by preparing the V45L/V61L double mutant whose reduction potential was measured to be 50 mV more negative than the value measured for the wild type protein. The negative shift in the reduction potential of the mutant protein was explained by the increased accessibility of water to the heme binding site, as observed in its X-ray crystal structure.

The reduction potential of cytochrome b5 is modulated by its exposed heme edge.,Rivera M, Seetharaman R, Girdhar D, Wirtz M, Zhang X, Wang X, White S Biochemistry. 1998 Feb 10;37(6):1485-94. PMID:9484218^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Rivera M, Seetharaman R, Girdhar D, Wirtz M, Zhang X, Wang X, White S. The reduction potential of cytochrome b5 is modulated by its exposed heme edge. Biochemistry. 1998 Feb 10;37(6):1485-94. PMID:9484218 doi:http://dx.doi.org/10.1021/bi972390g

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1awp"

Categories: Large Structures | Rattus norvegicus | Wang X | Zhang X

@@ Line 1: / Line 1: @@
 ==RAT OUTER MITOCHONDRIAL MEMBRANE CYTOCHROME B5==
-<StructureSection load='1awp' size='340' side='right' caption='[[1awp]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+<StructureSection load='1awp' size='340' side='right'caption='[[1awp]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1awp]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AWP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AWP FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1awp]] 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=1AWP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AWP 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">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</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=1awp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1awp OCA], [http://pdbe.org/1awp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1awp RCSB], [http://www.ebi.ac.uk/pdbsum/1awp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1awp ProSAT]</span></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=1awp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1awp OCA], [https://pdbe.org/1awp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1awp RCSB], [https://www.ebi.ac.uk/pdbsum/1awp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1awp ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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.
+[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 ==
 [[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/aw/1awp_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/aw/1awp_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 30: / Line 31: @@
 ==See Also==
-*[[Cytochrome b5|Cytochrome b5]]
+*[[Cytochrome b5 3D structures|Cytochrome b5 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Wang, X]]
+[[Category: Large Structures]]
-[[Category: Zhang, X]]
+[[Category: Rattus norvegicus]]
-[[Category: Cytochrome]]
+[[Category: Wang X]]
-[[Category: Electron transport]]
+[[Category: Zhang X]]
-[[Category: Heme]]

1awp

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Current revision

RAT OUTER MITOCHONDRIAL MEMBRANE CYTOCHROME B5

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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