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| | ==Cytochrome c prime from Alcaligenes xylosoxidans: Ferrous R124Q variant== | | ==Cytochrome c prime from Alcaligenes xylosoxidans: Ferrous R124Q variant== |
| - | <StructureSection load='2xld' size='340' side='right' caption='[[2xld]], [[Resolution|resolution]] 1.40Å' scene=''> | + | <StructureSection load='2xld' size='340' side='right'caption='[[2xld]], [[Resolution|resolution]] 1.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2xld]] 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=2XLD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XLD FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2xld]] 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=2XLD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XLD 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=SO4:SULFATE+ION'>SO4</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]] 1.4Å</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=PCA:PYROGLUTAMIC+ACID'>PCA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2xm0|2xm0]], [[2xlh|2xlh]], [[1cgo|1cgo]], [[2xm4|2xm4]], [[1e86|1e86]], [[2xl6|2xl6]], [[2xlx|2xlx]], [[1e85|1e85]], [[1cgn|1cgn]], [[2xlm|2xlm]], [[2xl5|2xl5]], [[2xle|2xle]], [[1e83|1e83]], [[2xlw|2xlw]], [[2xl8|2xl8]], [[1e84|1e84]], [[2xlv|2xlv]], [[2xlo|2xlo]]</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=2xld FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xld OCA], [https://pdbe.org/2xld PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xld RCSB], [https://www.ebi.ac.uk/pdbsum/2xld PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xld 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=2xld FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xld OCA], [http://pdbe.org/2xld PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xld RCSB], [http://www.ebi.ac.uk/pdbsum/2xld PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xld 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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| | ==See Also== | | ==See Also== |
| - | *[[Cytochrome c|Cytochrome c]] | + | *[[Cytochrome C 3D structures|Cytochrome C 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Achromobacter xylosoxidans yabuuchi and ohyama 1971]] | + | [[Category: Achromobacter xylosoxidans]] |
| - | [[Category: Antonyuk, S V]] | + | [[Category: Large Structures]] |
| - | [[Category: Hasnain, S S]] | + | [[Category: Antonyuk SV]] |
| - | [[Category: Hough, M A]] | + | [[Category: Hasnain SS]] |
| - | [[Category: 4-helix bundle]] | + | [[Category: Hough MA]] |
| - | [[Category: Electron transport]]
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| - | [[Category: Haemoprotein]]
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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
Hemoproteins play central roles in the formation and utilization of nitric oxide (NO) in cellular signalling, as well as in protection against nitrosative stress. Key to heme-nitrosyl function and reactivity is the Fe coordination number (5 or 6). For 5c-NO complexes, the potential exists for NO to bind on either heme face, as in the microbial cytochrome c' from Alcaligenes xylosoxidans (AxCYTcp), which forms a stable proximal 5c-NO complex via a distal 6c-NO intermediate and a putative dinitrosyl species. Strong parallels between the NO binding kinetics of AxCYTcp, the eukaryotic NO-sensor, soluble guanylate cyclase, and the ferrocytochrome c/cardiolipin complex have led to the suggestion that a distal to proximal NO switch could contribute to the selective ligand responses in gas-sensing hemoproteins. The proximal NO binding site in AxCYTcp is close to a conserved basic (Arg 124) residue that is postulated to modulate NO reactivity. We have replaced Arg 124 by five different amino acids and have determined high-resolution (1.07-1.40A) crystallographic structures with and without NO. These, together with kinetic and resonance Raman data, provide new insights into the mechanism of distal to proximal heme-NO conversion, including the determinants of Fe-His bond scission. The Arg124Ala variant allowed us to determine the structure of an analog of the previously unobserved key 5c-NO distal intermediate species. The very high-resolution structures combined with the extensive spectroscopic and kinetic data have allowed us to provide a fresh insight into heme reactivity towards NO, a reaction that is of wide importance in biology.
Distal to proximal NO conversion in hemoproteins: The role of the proximal pocket.,Hough MA, Antonyuk SV, Barbieri S, Rustage N, McKay AL, Servid AE, Eady RR, Andrew CR, Hasnain SS J Mol Biol. 2010 Nov 9. PMID:21073879[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hough MA, Antonyuk SV, Barbieri S, Rustage N, McKay AL, Servid AE, Eady RR, Andrew CR, Hasnain SS. Distal to proximal NO conversion in hemoproteins: The role of the proximal pocket. J Mol Biol. 2010 Nov 9. PMID:21073879 doi:10.1016/j.jmb.2010.10.035
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