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[[Image:1k3h.jpg|left|200px]]


{{Structure
==NMR Solution Structure of Oxidized Cytochrome c-553 from Bacillus pasteurii==
|PDB= 1k3h |SIZE=350|CAPTION= <scene name='initialview01'>1k3h</scene>
<StructureSection load='1k3h' size='340' side='right'caption='[[1k3h]]' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=HEC:HEME+C'>HEC</scene>
<table><tr><td colspan='2'>[[1k3h]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K3H FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1k3h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k3h OCA], [https://pdbe.org/1k3h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k3h RCSB], [https://www.ebi.ac.uk/pdbsum/1k3h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k3h ProSAT]</span></td></tr>
|RELATEDENTRY=[[1k3g|1K3G]], [[1c75|1C75]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1k3h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k3h OCA], [http://www.ebi.ac.uk/pdbsum/1k3h PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1k3h RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/CY553_SPOPA CY553_SPOPA]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k3/1k3h_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1k3h ConSurf].
<div style="clear:both"></div>


'''NMR Solution Structure of Oxidized Cytochrome c-553 from Bacillus pasteurii'''
==See Also==
 
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
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.
[[Category: Large Structures]]
 
==About this Structure==
1K3H 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].
 
==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:[http://www.ncbi.nlm.nih.gov/pubmed/11933230 11933230]
[[Category: Single protein]]
[[Category: Sporosarcina pasteurii]]
[[Category: Sporosarcina pasteurii]]
[[Category: Banci, L.]]
[[Category: Banci L]]
[[Category: Bertini, I.]]
[[Category: Bertini I]]
[[Category: Ciurli, S.]]
[[Category: Ciurli S]]
[[Category: Dikiy, A.]]
[[Category: Dikiy A]]
[[Category: Dittmer, J.]]
[[Category: Dittmer J]]
[[Category: Rosato, A.]]
[[Category: Rosato A]]
[[Category: Sciara, G.]]
[[Category: Sciara G]]
[[Category: Thompsett, A R.]]
[[Category: Thompsett AR]]
[[Category: bacillus pasteurii]]
[[Category: c-553]]
[[Category: cytochrome]]
[[Category: electron transfer]]
[[Category: heme]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:42:51 2008''

Latest revision as of 10:57, 3 April 2024

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

Structural highlights

1k3h is a 1 chain structure with sequence from Sporosarcina pasteurii. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CY553_SPOPA

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

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