1h32

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:17, 9 October 2024) (edit) (undo)
 
(15 intermediate revisions not shown.)
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=EDO:1,2-ETHANEDIOL'>EDO</scene> and <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>
-
}}
+
<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>
 +
</table>
 +
== 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/>
-
1H32 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: 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: EDO]]
+
-
[[Category: HEC]]
+
-
[[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 Thu Mar 20 11:31:31 2008''
+

Current revision

Reduced SoxAX complex from Rhodovulum sulfidophilum

PDB ID 1h32

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1h32"
Personal tools