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1zrt

From Proteopedia

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Rhodobacter capsulatus cytochrome bc1 complex with stigmatellin bound

Structural highlights

1zrt is a 6 chain structure with sequence from Rhodobacter capsulatus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.51Å
Ligands:	, , , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CYB_RHOCA Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Ubihydroquinone: cytochrome (cyt)c oxidoreductase, or cyt bc (1), is a widespread, membrane integral enzyme that plays a crucial role during photosynthesis and respiration. It is one of the major contributors of the electrochemical proton gradient, which is subsequently used for ATP synthesis. The simplest form of the cyt bc (1) is found in bacteria, and it contains only the three ubiquitously conserved catalytic subunits: the Fe-S protein, cyt b and cyt c (1). Here we present a preliminary X-ray structure of Rhodobacter capsulatus cyt bc (1) at 3.8 A and compare it to the available structures of its homologues from mitochondria and chloroplast. Using the bacterial enzyme structure, we highlight the structural similarities and differences that are found among the three catalytic subunits between the members of this family of enzymes. In addition, we discuss the locations of currently known critical mutations, and their implications in terms of the cyt bc (1) catalysis.

X-Ray Structure of Rhodobacter Capsulatus Cytochrome bc (1): Comparison with its Mitochondrial and Chloroplast Counterparts.,Berry EA, Huang LS, Saechao LK, Pon NG, Valkova-Valchanova M, Daldal F Photosynth Res. 2004;81(3):251-75. PMID:16034531^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Berry EA, Huang LS, Saechao LK, Pon NG, Valkova-Valchanova M, Daldal F. X-Ray Structure of Rhodobacter Capsulatus Cytochrome bc (1): Comparison with its Mitochondrial and Chloroplast Counterparts. Photosynth Res. 2004;81(3):251-75. PMID:16034531 doi:http://dx.doi.org/10.1023/B:PRES.0000036888.18223.0e

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1zrt"

@@ Line 3: / Line 3: @@
 <StructureSection load='1zrt' size='340' side='right'caption='[[1zrt]], [[Resolution|resolution]] 3.51&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1zrt]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/"rhodonostoc_capsulatum"_molisch_1907 "rhodonostoc capsulatum" molisch 1907]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZRT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZRT FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1zrt]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodobacter_capsulatus Rhodobacter capsulatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZRT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZRT FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PG6:1-(2-METHOXY-ETHOXY)-2-{2-[2-(2-METHOXY-ETHOXY]-ETHOXY}-ETHANE'>PG6</scene>, <scene name='pdbligand=SMA:STIGMATELLIN+A'>SMA</scene>, <scene name='pdbligand=UNL:UNKNOWN+LIGAND'>UNL</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]] 3.51&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[6xi0|6xi0]], [[1pp9|1pp9]], [[1kb9|1kb9]], [[2qjy|2qjy]], [[2yiu|2yiu]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PG6:1-(2-METHOXY-ETHOXY)-2-{2-[2-(2-METHOXY-ETHOXY]-ETHOXY}-ETHANE'>PG6</scene>, <scene name='pdbligand=SMA:STIGMATELLIN+A'>SMA</scene>, <scene name='pdbligand=UNL:UNKNOWN+LIGAND'>UNL</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">petB, cytB, RCAP_rcc02769 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1061 "Rhodonostoc capsulatum" Molisch 1907]), petC, RCAP_rcc02770 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1061 "Rhodonostoc capsulatum" Molisch 1907]), petA, fbcF, RCAP_rcc02768 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1061 "Rhodonostoc capsulatum" Molisch 1907])</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Quinol--cytochrome-c_reductase Quinol--cytochrome-c reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=7.1.1.8 7.1.1.8] </span></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=1zrt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zrt OCA], [https://pdbe.org/1zrt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zrt RCSB], [https://www.ebi.ac.uk/pdbsum/1zrt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zrt ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/CYB_RHOCB CYB_RHOCB]] Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. [[https://www.uniprot.org/uniprot/UCRI_RHOCB UCRI_RHOCB]] Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. [[https://www.uniprot.org/uniprot/CY1_RHOCB CY1_RHOCB]] Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. c1 functions as an electron donor to cytochrome c.
+[https://www.uniprot.org/uniprot/CYB_RHOCA CYB_RHOCA] Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis (By similarity).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 34: / Line 32: @@
 ==See Also==
 *[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
+*[[Cytochrome bc1 3D structures|Cytochrome bc1 3D structures]]
 *[[Cytochrome bc1 complex|Cytochrome bc1 complex]]
 == References ==
@@ Line 39: / Line 38: @@
 __TOC__
 </StructureSection>
-[[Category: Rhodonostoc capsulatum molisch 1907]]
 [[Category: Large Structures]]
-[[Category: Quinol--cytochrome-c reductase]]
+[[Category: Rhodobacter capsulatus]]
-[[Category: Berry, E A]]
+[[Category: Berry EA]]
-[[Category: Daldal, F]]
+[[Category: Daldal F]]
-[[Category: Huang, L S]]
+[[Category: Huang LS]]
-[[Category: Pon, N G]]
+[[Category: Pon NG]]
-[[Category: Saechao, L K]]
+[[Category: Saechao LK]]
-[[Category: Valkova-Valchanov, M]]
+[[Category: Valkova-Valchanov M]]
-[[Category: Complex iii]]
-[[Category: Cytochrome b]]
-[[Category: Cytochrome bc1]]
-[[Category: Cytochrome c1]]
-[[Category: Electron transport]]
-[[Category: Heme protein]]
-[[Category: Membrane protein]]
-[[Category: Oxidoreductase]]
-[[Category: Redox enzyme]]
-[[Category: Respiratory chain]]
-[[Category: Rieske iron sulfur protein]]
-[[Category: Stigmatellin]]

1zrt

From Proteopedia

Current revision

Rhodobacter capsulatus cytochrome bc1 complex with stigmatellin bound

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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