1sh4: Difference between revisions

Revision as of 12:22, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1sh4.png

Template:STRUCTURE 1sh4

Solution structure of oxidized bovine microsomal cytochrome B5 Mutant V45HSolution structure of oxidized bovine microsomal cytochrome B5 Mutant V45H

Template:ABSTRACT PUBMED 15273310

About this StructureAbout this Structure

1SH4 is a Single protein structure of sequence from Bos taurus. Full experimental information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Sun Jul 27 12:22:06 2008

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 {{STRUCTURE_1sh4|  PDB=1sh4  |  SCENE=  }}
-'''Solution structure of oxidized bovine microsomal cytochrome B5 Mutant V45H'''
+===Solution structure of oxidized bovine microsomal cytochrome B5 Mutant V45H===
-==Overview==
+<!--
-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 line below this paragraph, {{ABSTRACT_PUBMED_15273310}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15273310 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_15273310}}
 ==About this Structure==
-SH4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SH4 OCA].
+SH4 is a [[Single protein]] structure of sequence from [http://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].
 ==Reference==
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 [[Category: Five sheet]]
 [[Category: Heme ring]]
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