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2bgv

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[[Image:2bgv.gif|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bgv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bgv OCA], [http://www.ebi.ac.uk/pdbsum/2bgv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bgv RCSB]</span>
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'''X-RAY STRUCTURE OF FERRIC CYTOCHROME C-550 FROM PARACOCCUS VERSUTUS'''
'''X-RAY STRUCTURE OF FERRIC CYTOCHROME C-550 FROM PARACOCCUS VERSUTUS'''
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[[Category: Ubbink, M.]]
[[Category: Ubbink, M.]]
[[Category: Worrall, J A.R.]]
[[Category: Worrall, J A.R.]]
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[[Category: c-type cytochrome]]
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[[Category: C-type cytochrome]]
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[[Category: electron transfer]]
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[[Category: Electron transfer]]
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[[Category: heme group]]
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[[Category: Heme group]]
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[[Category: pyrrolidone carboxylic acid]]
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[[Category: Pyrrolidone carboxylic acid]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:16:11 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:06:12 2008''
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Revision as of 17:16, 3 May 2008

Template:STRUCTURE 2bgv

X-RAY STRUCTURE OF FERRIC CYTOCHROME C-550 FROM PARACOCCUS VERSUTUS


Overview

The structure of cytochrome c-550 from the nonphotosynthetic bacteria Paraccocus versutus has been solved by X-ray crystallography to 1.90 A resolution, and reveals a high structural homology to other bacterial cytochromes c(2). The effect of replacing the axial heme-iron methionine ligand with a lysine residue on protein structure and unfolding has been assessed using the M100K variant. From X-ray structures at 1.95 and 1.55 A resolution it became clear that the amino group of the lysine side chain coordinates to the heme-iron. Structural differences compared to the wild-type protein are confined to the lysine ligand loop connecting helices four and five. In the heme cavity an additional water molecule is found which participates in an H-bonding interaction with the lysine ligand. Under cryo-conditions extra electron density in the lysine ligand loop is revealed, leading to residues K97 to T101 being modeled with a double main-chain conformation. Upon unfolding, dissociation of the lysine ligand from the heme-iron is shown to be pH dependent, with NMR data consistent with the occurrence of a ligand exchange mechanism similar to that seen for the wild-type protein.

About this Structure

2BGV is a Single protein structure of sequence from Paracoccus versutus. Full crystallographic information is available from OCA.

Reference

The effect of replacing the axial methionine ligand with a lysine residue in cytochrome c-550 from Paracoccus versutus assessed by X-ray crystallography and unfolding., Worrall JA, van Roon AM, Ubbink M, Canters GW, FEBS J. 2005 May;272(10):2441-55. PMID:15885094 Page seeded by OCA on Sat May 3 20:16:11 2008

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