2bh5: Difference between revisions

Revision as of 13:39, 28 July 2008

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File:2bh5.png

Template:STRUCTURE 2bh5

X-RAY STRUCTURE OF THE M100K VARIANT OF FERRIC CYT C-550 FROM PARACOCCUS VERSUTUS DETERMINED AT 295 K.X-RAY STRUCTURE OF THE M100K VARIANT OF FERRIC CYT C-550 FROM PARACOCCUS VERSUTUS DETERMINED AT 295 K.

Template:ABSTRACT PUBMED 15885094

About this StructureAbout this Structure

2BH5 is a Single protein structure of sequence from Paracoccus versutus. Full crystallographic information is available from OCA.

ReferenceReference

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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''X-RAY STRUCTURE OF THE M100K VARIANT OF FERRIC CYT C-550 FROM PARACOCCUS VERSUTUS DETERMINED AT 295 K.'''
+===X-RAY STRUCTURE OF THE M100K VARIANT OF FERRIC CYT C-550 FROM PARACOCCUS VERSUTUS DETERMINED AT 295 K.===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15885094}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_15885094}}
 ==About this Structure==
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 [[Category: Heme]]
 [[Category: Pyrrolidone carboxylic acid]]
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