1kx7: Difference between revisions
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<StructureSection load='1kx7' size='340' side='right' caption='[[1kx7]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''> | <StructureSection load='1kx7' size='340' side='right' caption='[[1kx7]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1kx7]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1kx7]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"pseudomonas_putrefaciens"_(derby_and_hammer)_long_and_hammer_1941 "pseudomonas putrefaciens" (derby and hammer) long and hammer 1941]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KX7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KX7 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1kx2|1kx2]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1kx2|1kx2]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ScyA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=24 | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ScyA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=24 "Pseudomonas putrefaciens" (Derby and Hammer) Long and Hammer 1941])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kx7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kx7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1kx7 RCSB], [http://www.ebi.ac.uk/pdbsum/1kx7 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kx7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kx7 OCA], [http://pdbe.org/1kx7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kx7 RCSB], [http://www.ebi.ac.uk/pdbsum/1kx7 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1kx7" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bartalesi, I]] | [[Category: Bartalesi, I]] | ||
[[Category: Bertini, I]] | [[Category: Bertini, I]] | ||
Revision as of 09:32, 10 September 2015
Family of 30 conformers of a mono-heme ferrocytochrome c from Shewanella putrefaciens solved by NMRFamily of 30 conformers of a mono-heme ferrocytochrome c from Shewanella putrefaciens solved by NMR
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedWithin the frame of the characterization of the structure and function of cytochromes c, an 81-amino acid cytochrome c was identified in the genome of Shewanella putrefaciens. Because of the scarce information about bacterial cytochromes of this type and the large variability in sequences and possibly function, we decided to proceed to its structural characterization. This protein was expressed in Escherichia coli and purified. The oxidized species is largely high spin, with a detached methionine, whereas the reduced species has the classical His/Met axial ligation to iron. The NMR solution structure of the reduced form was determined on a (15)N-labeled sample, for which 99% of all non-proline backbone (1)H and (15)N resonances have been assigned. One thousand three hundred two meaningful NOEs, out of 1775 NOEs, together with 66 dihedral angles provide a structure with rmsd values from the mean of 0.50 and 0.96 A for backbone and all heavy atoms, respectively. A search of gene banks allowed us to locate 10 different cytochromes c, the sequences of which are more than 30% identical to that of the S. putrefacienscytochrome. For two of them, the structures are known. The structures of the others have been modeled by using the available templates and internally validated. Structural similarities in terms of surface properties account for their biophysical features and provide hints about the function. Solution structure of a monoheme ferrocytochrome c from Shewanella putrefaciens and structural analysis of sequence-similar proteins: functional implications.,Bartalesi I, Bertini I, Hajieva P, Rosato A, Vasos PR Biochemistry. 2002 Apr 23;41(16):5112-9. PMID:11955059[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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