1e86: Difference between revisions

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-[[Image:1e86.jpg|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_1e86", creates the "Structure Box" on the page.
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-{{STRUCTURE_1e86|  PDB=1e86  |  SCENE=  }}
-'''CYTOCHROME C' FROM ALCALIGENES XYLOSOXIDANS-REDUCED STRUCTURE WITH CO BOUND TO DISTAL SIDE OF HEME'''
+==Cytochrome c' from Alcaligenes xylosoxidans - reduced structure with CO bound to distal side of heme==
+<StructureSection load='1e86' size='340' side='right'caption='[[1e86]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1e86]] 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=1E86 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E86 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></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=1e86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e86 OCA], [https://pdbe.org/1e86 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e86 RCSB], [https://www.ebi.ac.uk/pdbsum/1e86 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e86 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.
+== 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/e8/1e86_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=1e86 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Microbial cytochromes c' contain a 5-coordinate His-ligated heme that forms stable adducts with nitric oxide (NO) and carbon monoxide (CO), but not with dioxygen. We report the 1.95 and 1.35 A resolution crystal structures of the CO- and NO-bound forms of the reduced protein from Alcaligenes xylosoxidans. NO disrupts the His-Fe bond and binds in a novel mode to the proximal face of the heme, giving a 5-coordinate species. In contrast, CO binds 6-coordinate on the distal side. A second CO molecule, not bound to the heme, is located in the proximal pocket. Since the unusual spectroscopic properties of cytochromes c' are shared by soluble guanylate cyclase (sGC), our findings have potential implications for the activation of sGC induced by the binding of NO or CO to the heme domain.
-==Overview==
+Unprecedented proximal binding of nitric oxide to heme: implications for guanylate cyclase.,Lawson DM, Stevenson CE, Andrew CR, Eady RR EMBO J. 2000 Nov 1;19(21):5661-71. PMID:11060017<ref>PMID:11060017</ref>
-Microbial cytochromes c' contain a 5-coordinate His-ligated heme that forms stable adducts with nitric oxide (NO) and carbon monoxide (CO), but not with dioxygen. We report the 1.95 and 1.35 A resolution crystal structures of the CO- and NO-bound forms of the reduced protein from Alcaligenes xylosoxidans. NO disrupts the His-Fe bond and binds in a novel mode to the proximal face of the heme, giving a 5-coordinate species. In contrast, CO binds 6-coordinate on the distal side. A second CO molecule, not bound to the heme, is located in the proximal pocket. Since the unusual spectroscopic properties of cytochromes c' are shared by soluble guanylate cyclase (sGC), our findings have potential implications for the activation of sGC induced by the binding of NO or CO to the heme domain.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-E86 is a [[Single protein]] structure of 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=1E86 OCA].
+</div>
+<div class="pdbe-citations 1e86" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-Unprecedented proximal binding of nitric oxide to heme: implications for guanylate cyclase., Lawson DM, Stevenson CE, Andrew CR, Eady RR, EMBO J. 2000 Nov 1;19(21):5661-71. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11060017 11060017]
+*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Achromobacter xylosoxidans]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Andrew, C R.]]
+[[Category: Andrew CR]]
-[[Category: Eady, R R.]]
+[[Category: Eady RR]]
-[[Category: Lawson, D M.]]
+[[Category: Lawson DM]]
-[[Category: Stevenson, C E.M.]]
+[[Category: Stevenson CEM]]
-[[Category: 4-helix bundle]]
-[[Category: Carbon monoxide]]
-[[Category: Cytochrome]]
-[[Category: Heme]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:47:00 2008''