1h32: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1h32.jpg|left|200px]]
- {{Structure
+==Reduced SoxAX complex from Rhodovulum sulfidophilum==
-|PDB= 1h32 |SIZE=350|CAPTION= <scene name='initialview01'>1h32</scene>, resolution 1.5&Aring;
+<StructureSection load='1h32' size='340' side='right'caption='[[1h32]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
-|SITE= <scene name='pdbsite=EA1:Hec+Binding+Site+For+Chain+B'>EA1</scene>
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=CSS:S-MERCAPTOCYSTEINE'>CSS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>
+<table><tr><td colspan='2'>[[1h32]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodovulum_sulfidophilum Rhodovulum sulfidophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H32 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H32 FirstGlance]. <br>
-|ACTIVITY=
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
-|GENE=
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSS:S-MERCAPTOCYSTEINE'>CSS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr>
-|DOMAIN=
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1h32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h32 OCA], [https://pdbe.org/1h32 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h32 RCSB], [https://www.ebi.ac.uk/pdbsum/1h32 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h32 ProSAT]</span></td></tr>
-|RELATEDENTRY=
+</table>
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h32 OCA], [http://www.ebi.ac.uk/pdbsum/1h32 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1h32 RCSB]</span>
+== Function ==
-}}
+[https://www.uniprot.org/uniprot/Q939U4_RHOSU Q939U4_RHOSU]
+== 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/h3/1h32_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1h32 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Reduced inorganic sulfur compounds are utilized by many bacteria as electron donors to photosynthetic or respiratory electron transport chains. This metabolism is a key component of the biogeochemical sulfur cycle. The SoxAX protein is a heterodimeric c-type cytochrome involved in thiosulfate oxidation. The crystal structures of SoxAX from the photosynthetic bacterium Rhodovulum sulfidophilum have been solved at 1.75 A resolution in the oxidized state and at 1.5 A resolution in the dithionite-reduced state, providing the first structural insights into the enzymatic oxidation of thiosulfate. The SoxAX active site contains a haem with unprecedented cysteine persulfide (cysteine sulfane) coordination. This unusual post-translational modification is also seen in sulfurtransferases such as rhodanese. Intriguingly, this enzyme shares further active site characteristics with SoxAX such as an adjacent conserved arginine residue and a strongly positive electrostatic potential. These similarities have allowed us to suggest a catalytic mechanism for enzymatic thiosulfate oxidation. The atomic coordinates and experimental structure factors have been deposited in the PDB with the accession codes 1H31, 1H32 and 1H33.
-'''REDUCED SOXAX COMPLEX FROM RHODOVULUM SULFIDOPHILUM'''
+Structural basis for the oxidation of thiosulfate by a sulfur cycle enzyme.,Bamford VA, Bruno S, Rasmussen T, Appia-Ayme C, Cheesman MR, Berks BC, Hemmings AM EMBO J. 2002 Nov 1;21(21):5599-610. PMID:12411478<ref>PMID:12411478</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1h32" style="background-color:#fffaf0;"></div>
-==Overview==
+==See Also==
-Reduced inorganic sulfur compounds are utilized by many bacteria as electron donors to photosynthetic or respiratory electron transport chains. This metabolism is a key component of the biogeochemical sulfur cycle. The SoxAX protein is a heterodimeric c-type cytochrome involved in thiosulfate oxidation. The crystal structures of SoxAX from the photosynthetic bacterium Rhodovulum sulfidophilum have been solved at 1.75 A resolution in the oxidized state and at 1.5 A resolution in the dithionite-reduced state, providing the first structural insights into the enzymatic oxidation of thiosulfate. The SoxAX active site contains a haem with unprecedented cysteine persulfide (cysteine sulfane) coordination. This unusual post-translational modification is also seen in sulfurtransferases such as rhodanese. Intriguingly, this enzyme shares further active site characteristics with SoxAX such as an adjacent conserved arginine residue and a strongly positive electrostatic potential. These similarities have allowed us to suggest a catalytic mechanism for enzymatic thiosulfate oxidation. The atomic coordinates and experimental structure factors have been deposited in the PDB with the accession codes 1H31, 1H32 and 1H33.
+*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
+== References ==
-==About this Structure==
+<references/>
-H32 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Rhodovulum_sulfidophilum Rhodovulum sulfidophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H32 OCA].
+__TOC__
+</StructureSection>
-==Reference==
+[[Category: Large Structures]]
-Structural basis for the oxidation of thiosulfate by a sulfur cycle enzyme., Bamford VA, Bruno S, Rasmussen T, Appia-Ayme C, Cheesman MR, Berks BC, Hemmings AM, EMBO J. 2002 Nov 1;21(21):5599-610. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12411478 12411478]
-[[Category: Protein complex]]
 [[Category: Rhodovulum sulfidophilum]]
-[[Category: Appia-Ayme, C.]]
+[[Category: Appia-Ayme C]]
-[[Category: Bamford, V A.]]
+[[Category: Bamford VA]]
-[[Category: Berks, B C.]]
+[[Category: Berks BC]]
-[[Category: Bruno, S.]]
+[[Category: Bruno S]]
-[[Category: Cheesman, M R.]]
+[[Category: Cheesman MR]]
-[[Category: Hemmings, A M.]]
+[[Category: Hemmings AM]]
-[[Category: Rasmussen, T.]]
+[[Category: Rasmussen T]]
-[[Category: cysteine persulfide heme ligand]]
-[[Category: cytochrome c]]
-[[Category: soxax complex]]
-[[Category: sulfur cycle]]
-[[Category: thiosulfate oxidation]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:56:42 2008''