1e8e
From Proteopedia
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- | [[Image:1e8e.gif|left|200px]] | + | [[Image:1e8e.gif|left|200px]] |
- | + | ||
- | '''SOLUTION STRUCTURE OF METHYLOPHILUS METHYLOTROPHUS CYTOCHROME C''. INSIGHTS INTO THE STRUCTURAL BASIS OF HAEM-LIGAND DETACHMENT''' | + | {{Structure |
+ | |PDB= 1e8e |SIZE=350|CAPTION= <scene name='initialview01'>1e8e</scene> | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=HEC:HEME C'>HEC</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''SOLUTION STRUCTURE OF METHYLOPHILUS METHYLOTROPHUS CYTOCHROME C''. INSIGHTS INTO THE STRUCTURAL BASIS OF HAEM-LIGAND DETACHMENT''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1E8E is a [ | + | 1E8E is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Methylophilus_methylotrophus Methylophilus methylotrophus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E8E OCA]. |
==Reference== | ==Reference== | ||
- | Solution structure of Methylophilus methylotrophus cytochrome c": insights into the structural basis of haem-ligand detachment., Brennan L, Turner DL, Fareleira P, Santos H, J Mol Biol. 2001 Apr 27;308(2):353-65. PMID:[http:// | + | Solution structure of Methylophilus methylotrophus cytochrome c": insights into the structural basis of haem-ligand detachment., Brennan L, Turner DL, Fareleira P, Santos H, J Mol Biol. 2001 Apr 27;308(2):353-65. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11327772 11327772] |
[[Category: Methylophilus methylotrophus]] | [[Category: Methylophilus methylotrophus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Turner, D L.]] | [[Category: Turner, D L.]] | ||
[[Category: HEC]] | [[Category: HEC]] | ||
- | [[Category: cytochrome c'']] | + | [[Category: cytochrome c's']] |
[[Category: ligand detachment]] | [[Category: ligand detachment]] | ||
[[Category: paramagnetic]] | [[Category: paramagnetic]] | ||
[[Category: redox-bohr effect]] | [[Category: redox-bohr effect]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:51:31 2008'' |
Revision as of 08:51, 20 March 2008
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Coordinates: | save as pdb, mmCIF, xml |
SOLUTION STRUCTURE OF METHYLOPHILUS METHYLOTROPHUS CYTOCHROME C. INSIGHTS INTO THE STRUCTURAL BASIS OF HAEM-LIGAND DETACHMENT
Overview
Cytochrome c" from Methylophilus methylotrophus is a monohaem protein with 124 amino acid residues. The iron has two histidine ligands in the oxidised form, one of which detaches and picks up a proton when the protein is reduced. Thus, both forms are paramagnetic. The structure of the oxidised form in solution, determined from NMR data is presented. The family of structures has an average backbone rmsd value of 0.53 A, and a heavy atom rmsd value of 0.95 A, within a target function range of 32 %. This structure is related to class I cytochromes with an additional helix at the N terminus. The haem-binding site occurs in a domain essentially lacking secondary structure motifs and the axial histidinyl residues were found in an unusual near perpendicular orientation. Moreover, a disulfide bridge is present, an uncommon structural feature among c-type cytochromes. The disulfide bridge, linking cysteine residues 96 and 104, forms a loop that confers rigidity and is essential to the detachment of the axial histidine (His95) as demonstrated by chemical disruption of the S-S bond. A route for protonation of the distal histidine involving haem propionate 17 is proposed and discussed in the light of available models for complex membrane proton pumps.
About this Structure
1E8E is a Single protein structure of sequence from Methylophilus methylotrophus. Full crystallographic information is available from OCA.
Reference
Solution structure of Methylophilus methylotrophus cytochrome c": insights into the structural basis of haem-ligand detachment., Brennan L, Turner DL, Fareleira P, Santos H, J Mol Biol. 2001 Apr 27;308(2):353-65. PMID:11327772
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