1k3h
From Proteopedia
(New page: 200px<br /><applet load="1k3h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k3h" /> '''NMR Solution Structure of Oxidized Cytochrom...) |
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'''NMR Solution Structure of Oxidized Cytochrome c-553 from Bacillus pasteurii'''<br /> | '''NMR Solution Structure of Oxidized Cytochrome c-553 from Bacillus pasteurii'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The solution structure of oxidized cytochrome c(553) (71 amino acid | + | 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 (>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. |
==About this Structure== | ==About this Structure== | ||
| - | 1K3H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sporosarcina_pasteurii Sporosarcina pasteurii] with HEC as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1K3H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sporosarcina_pasteurii Sporosarcina pasteurii] with <scene name='pdbligand=HEC:'>HEC</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K3H OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Rosato, A.]] | [[Category: Rosato, A.]] | ||
[[Category: Sciara, G.]] | [[Category: Sciara, G.]] | ||
| - | [[Category: Thompsett, A | + | [[Category: Thompsett, A R.]] |
[[Category: HEC]] | [[Category: HEC]] | ||
[[Category: bacillus pasteurii]] | [[Category: bacillus pasteurii]] | ||
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[[Category: heme]] | [[Category: heme]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:29:43 2008'' |
Revision as of 11:29, 21 February 2008
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NMR Solution Structure of Oxidized Cytochrome c-553 from Bacillus pasteurii
Overview
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 (>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.
About this Structure
1K3H is a Single protein structure of sequence from Sporosarcina pasteurii with as ligand. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 13:29:43 2008
Categories: Single protein | Sporosarcina pasteurii | Banci, L. | Bertini, I. | Ciurli, S. | Dikiy, A. | Dittmer, J. | Rosato, A. | Sciara, G. | Thompsett, A R. | HEC | Bacillus pasteurii | C-553 | Cytochrome | Electron transfer | Heme
