1bfx

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(Difference between revisions)

Revision as of 06:59, 24 February 2021

THE SOLUTION NMR STRUCTURE OF THE B FORM OF OXIDIZED RAT MICROSOMAL CYTOCHROME B5, MINIMIZED AVERAGE STRUCTURE

Structural highlights

1bfx is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CYB5_RAT] Cytochrome b5 is a membrane bound hemoprotein which function as an electron carrier for several membrane bound oxygenases. It is also involved in several steps of the sterol biosynthesis pathway, particularly in the C-6 double bond introduction during the C-6 desaturation.

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

Cytochrome b5 in solution has two isomers (A and B) differing by a 180 degrees rotation of the protoporphyrin IX plane around the axis defined by the alpha and gamma meso protons. Homonuclear and heteronuclear NMR spectroscopy has been employed in order to solve the solution structure of the minor (B) form of the oxidized state of the protein and to probe its backbone dynamics in the microsecond--ms timescale in both oxidation states. A family of 40 conformers has been obtained using 1302 meaningful NOEs and 220 pseudocontact shifts and is characterized by high quality and good resolution (rmsd to the mean structure of 0.055 +/- 0.009 nm and 0.103 +/- 0.011 nm for backbone and heavy atoms, respectively). Extensive comparisons of the structural and dynamics changes associated with the A-to-B form interconversion for both oxidation states were subsequently performed. Propionate 6 experiences a redox-state-dependent reorientation as does propionate 7 in the A form. Significant insights are obtained into the role of the protein frame for efficient biological function and backbone mobility is proposed to be one of the factors that could control the reduction potential of the heme.

Solution structure of the B form of oxidized rat microsomal cytochrome b5 and backbone dynamics via 15N rotating-frame NMR-relaxation measurements. Biological implications.,Arnesano F, Banci L, Bertini I, Felli IC, Koulougliotis D Eur J Biochem. 1999 Mar;260(2):347-54. PMID:10095768^[1]

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

References

↑ Arnesano F, Banci L, Bertini I, Felli IC, Koulougliotis D. Solution structure of the B form of oxidized rat microsomal cytochrome b5 and backbone dynamics via 15N rotating-frame NMR-relaxation measurements. Biological implications. Eur J Biochem. 1999 Mar;260(2):347-54. PMID:10095768

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/1bfx"

@@ Line 3: / Line 3: @@
 <StructureSection load='1bfx' size='340' side='right'caption='[[1bfx]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1bfx]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BFX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BFX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1bfx]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BFX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BFX 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='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=1bfx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bfx OCA], [http://pdbe.org/1bfx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bfx RCSB], [http://www.ebi.ac.uk/pdbsum/1bfx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bfx 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=1bfx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bfx OCA], [https://pdbe.org/1bfx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bfx RCSB], [https://www.ebi.ac.uk/pdbsum/1bfx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bfx ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CYB5_RAT CYB5_RAT]] Cytochrome b5 is a membrane bound hemoprotein which function as an electron carrier for several membrane bound oxygenases. It is also involved in several steps of the sterol biosynthesis pathway, particularly in the C-6 double bond introduction during the C-6 desaturation.
+[[https://www.uniprot.org/uniprot/CYB5_RAT CYB5_RAT]] Cytochrome b5 is a membrane bound hemoprotein which function as an electron carrier for several membrane bound oxygenases. It is also involved in several steps of the sterol biosynthesis pathway, particularly in the C-6 double bond introduction during the C-6 desaturation.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 30: / Line 30: @@
 ==See Also==
-*[[Cytochrome b5|Cytochrome b5]]
+*[[Cytochrome b5 3D structures|Cytochrome b5 3D structures]]
 == References ==
 <references/>

1bfx

From Proteopedia

Revision as of 06:59, 24 February 2021

THE SOLUTION NMR STRUCTURE OF THE B FORM OF OXIDIZED RAT MICROSOMAL CYTOCHROME B5, MINIMIZED AVERAGE STRUCTURE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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