1k3h: Difference between revisions

Revision as of 02:23, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1k3h.png

Template:STRUCTURE 1k3h

NMR Solution Structure of Oxidized Cytochrome c-553 from Bacillus pasteuriiNMR Solution Structure of Oxidized Cytochrome c-553 from Bacillus pasteurii

Template:ABSTRACT PUBMED 11933230

About this StructureAbout this Structure

1K3H is a Single protein structure of sequence from Sporosarcina pasteurii. Full experimental information is available from OCA.

ReferenceReference

NMR solution structure, backbone mobility, and homology modeling of c-type cytochromes from gram-positive bacteria., Banci L, Bertini I, Ciurli S, Dikiy A, Dittmer J, Rosato A, Sciara G, Thompsett AR, Chembiochem. 2002 Apr 2;3(4):299-310. PMID:11933230

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OCA

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-'''NMR Solution Structure of Oxidized Cytochrome c-553 from Bacillus pasteurii'''
+===NMR Solution Structure of Oxidized Cytochrome c-553 from Bacillus pasteurii===
-==Overview==
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-The solution structure of oxidized cytochrome c(553) (71 amino acid residues) from the Gram-positive bacterium Bacillus pasteurii is here reported and compared with the available crystal structure. The solution structure is obtained from 1609 meaningful NOE data (22.7 per residue), 76 dihedral angles, and 59 pseudocontact shifts. The root mean square deviations from the average structure are 0.25+/-0.07 and 0.59+/-0.13 A for the backbone and all heavy atoms, respectively, and the quality assessment of the structure is satisfactory. The solution structure closely reproduces the fold observed in the crystal structure. The backbone mobility was then investigated through amide (15)N relaxation rate and (15)N-(1)H NOE measurements. The protein is rigid in both the sub-nanosecond and millisecond time scales, probably due to the relatively large heme:number of amino acids ratio. Modeling of eight c-type cytochromes from other Gram-positive bacteria with a high sequence identity (&gt;30 %) to the present cytochrome c(553) was performed. Analysis of consensus features accounts for the relatively low reduction potential as being due to extensive heme hydration and indicates residues 34-35, 44-46, 69-72, and 75 as a conserved hydrophobic patch for the interaction with a protein partner. At variance with mitochondrial c-type cytochrome, this protein does not experience pH-dependent coordination equilibria. The reasons for this difference are analyzed.
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+{{ABSTRACT_PUBMED_11933230}}
 ==About this Structure==
-K3H is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sporosarcina_pasteurii Sporosarcina pasteurii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K3H OCA].
+K3H is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sporosarcina_pasteurii Sporosarcina pasteurii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K3H OCA].
 ==Reference==
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 [[Category: Electron transfer]]
 [[Category: Heme]]
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