2xm0: Difference between revisions

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-[[Image:2xm0.png|left|200px]]
-<!--
+==Cytochrome c prime from Alcaligenes xylosoxidans: Ferrous R124K variant==
-The line below this paragraph, containing "STRUCTURE_2xm0", creates the "Structure Box" on the page.
+<StructureSection load='2xm0' size='340' side='right'caption='[[2xm0]], [[Resolution|resolution]] 1.25&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2xm0]] 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=2XM0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XM0 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.25&#8491;</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></td></tr>
-{{STRUCTURE_2xm0|  PDB=2xm0  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2xm0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xm0 OCA], [https://pdbe.org/2xm0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xm0 RCSB], [https://www.ebi.ac.uk/pdbsum/2xm0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xm0 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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;">
+== 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.
-===CYTOCHROME C PRIME FROM ALCALIGENES XYLOSOXIDANS: FERROUS R124K VARIANT===
+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<ref>PMID:21073879</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2xm0" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_21073879}}, adds the Publication Abstract to the page
+*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 21073879 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_21073879}}
+__TOC__
+</StructureSection>
-==About this Structure==
-[[2xm0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Achromobacter_xylosoxidans Achromobacter xylosoxidans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XM0 OCA].
-==Reference==
-<ref group="xtra">PMID:21073879</ref><references group="xtra"/>
 [[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: Hough MA]]