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| | <StructureSection load='4cjg' size='340' side='right'caption='[[4cjg]], [[Resolution|resolution]] 1.26Å' scene=''> | | <StructureSection load='4cjg' size='340' side='right'caption='[[4cjg]], [[Resolution|resolution]] 1.26Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4cjg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"achromobacter_xylosoxidans"_yabuuchi_and_ohyama_1971 "achromobacter xylosoxidans" yabuuchi and ohyama 1971]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CJG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CJG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4cjg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Achromobacter_xylosoxidans Achromobacter xylosoxidans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CJG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CJG 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>, <scene name='pdbligand=NO:NITRIC+OXIDE'>NO</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.26Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=NO:NITRIC+OXIDE'>NO</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cip|4cip]]</td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4cjg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cjg OCA], [https://pdbe.org/4cjg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cjg RCSB], [https://www.ebi.ac.uk/pdbsum/4cjg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cjg ProSAT]</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=4cjg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cjg OCA], [http://pdbe.org/4cjg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cjg RCSB], [http://www.ebi.ac.uk/pdbsum/4cjg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cjg ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CYCP_ALCXX CYCP_ALCXX]] Cytochrome c' is the most widely occurring bacterial c-type cytochrome. Cytochromes c' are high-spin proteins and the heme has no sixth ligand. Their exact function is not known. | + | [https://www.uniprot.org/uniprot/CYCP_ALCXX CYCP_ALCXX] Cytochrome c' is the most widely occurring bacterial c-type cytochrome. Cytochromes c' are high-spin proteins and the heme has no sixth ligand. Their exact function is not known. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Achromobacter xylosoxidans yabuuchi and ohyama 1971]] | + | [[Category: Achromobacter xylosoxidans]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Antonyuk, S]] | + | [[Category: Antonyuk S]] |
| - | [[Category: Dworkowski, F]] | + | [[Category: Dworkowski F]] |
| - | [[Category: Fuchs, M]] | + | [[Category: Fuchs M]] |
| - | [[Category: Hough, M A]] | + | [[Category: Hough MA]] |
| - | [[Category: Kekilli, D]] | + | [[Category: Kekilli D]] |
| - | [[Category: Electron transport]]
| + | |
| - | [[Category: Nitrosyl]]
| + | |
| - | [[Category: Proximal]]
| + | |
| - | [[Category: Resonance raman]]
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| Structural highlights
Function
CYCP_ALCXX Cytochrome c' is the most widely occurring bacterial c-type cytochrome. Cytochromes c' are high-spin proteins and the heme has no sixth ligand. Their exact function is not known.
Publication Abstract from PubMed
It is crucial to assign the correct redox and ligand states to crystal structures of proteins with an active redox centre to gain valid functional information and prevent the misinterpretation of structures. Single-crystal spectroscopies, particularly when applied in situ at macromolecular crystallography beamlines, allow spectroscopic investigations of redox and ligand states and the identification of reaction intermediates in protein crystals during the collection of structural data. Single-crystal resonance Raman spectroscopy was carried out in combination with macromolecular crystallography on Swiss Light Source beamline X10SA using cytochrome c' from Alcaligenes xylosoxidans. This allowed the fingerprinting and validation of different redox and ligand states, identification of vibrational modes and identification of intermediates together with monitoring of radiation-induced changes. This combined approach provides a powerful tool to obtain complementary data and correctly assign the true oxidation and ligand state(s) in redox-protein crystals.
Fingerprinting redox and ligand states in haemprotein crystal structures using resonance Raman spectroscopy.,Kekilli D, Dworkowski FS, Pompidor G, Fuchs MR, Andrew CR, Antonyuk S, Strange RW, Eady RR, Hasnain SS, Hough MA Acta Crystallogr D Biol Crystallogr. 2014 May;70(Pt 5):1289-96. doi:, 10.1107/S1399004714004039. Epub 2014 Apr 29. PMID:24816098[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kekilli D, Dworkowski FS, Pompidor G, Fuchs MR, Andrew CR, Antonyuk S, Strange RW, Eady RR, Hasnain SS, Hough MA. Fingerprinting redox and ligand states in haemprotein crystal structures using resonance Raman spectroscopy. Acta Crystallogr D Biol Crystallogr. 2014 May;70(Pt 5):1289-96. doi:, 10.1107/S1399004714004039. Epub 2014 Apr 29. PMID:24816098 doi:http://dx.doi.org/10.1107/S1399004714004039
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