2bgv

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{{STRUCTURE_2bgv| PDB=2bgv | SCENE= }}
{{STRUCTURE_2bgv| PDB=2bgv | SCENE= }}
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'''X-RAY STRUCTURE OF FERRIC CYTOCHROME C-550 FROM PARACOCCUS VERSUTUS'''
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===X-RAY STRUCTURE OF FERRIC CYTOCHROME C-550 FROM PARACOCCUS VERSUTUS===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_15885094}}
==About this Structure==
==About this Structure==
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[[Category: Heme group]]
[[Category: Heme group]]
[[Category: Pyrrolidone carboxylic acid]]
[[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 Tue Jul 29 11:20:24 2008''

Revision as of 08:20, 29 July 2008

Image:2bgv.png

Template:STRUCTURE 2bgv

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

Template:ABSTRACT PUBMED 15885094

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

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