2bh4
From Proteopedia
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|PDB= 2bh4 |SIZE=350|CAPTION= <scene name='initialview01'>2bh4</scene>, resolution 1.55Å | |PDB= 2bh4 |SIZE=350|CAPTION= <scene name='initialview01'>2bh4</scene>, resolution 1.55Å | ||
|SITE= <scene name='pdbsite=AC1:Hec+Binding+Site+For+Chain+X'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Hec+Binding+Site+For+Chain+X'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=HEC:HEME C'>HEC</scene> | + | |LIGAND= <scene name='pdbligand=HEC:HEME+C'>HEC</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bh4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bh4 OCA], [http://www.ebi.ac.uk/pdbsum/2bh4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bh4 RCSB]</span> | ||
}} | }} | ||
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[[Category: Ubbink, M.]] | [[Category: Ubbink, M.]] | ||
[[Category: Worrall, J A.R.]] | [[Category: Worrall, J A.R.]] | ||
| - | [[Category: HEC]] | ||
[[Category: axial ligand]] | [[Category: axial ligand]] | ||
[[Category: c-type cytochrome]] | [[Category: c-type cytochrome]] | ||
| Line 33: | Line 35: | ||
[[Category: pyrrolidone carboxylic acid]] | [[Category: pyrrolidone carboxylic acid]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:06:19 2008'' |
Revision as of 23:06, 30 March 2008
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| , resolution 1.55Å | |||||||
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| Sites: | |||||||
| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
X-RAY STRUCTURE OF THE M100K VARIANT OF FERRIC CYT C-550 FROM PARACOCCUS VERSUTUS DETERMINED AT 100 K.
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
2BH4 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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