2yiu

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Revision as of 19:40, 11 August 2016

X-RAY STRUCTURE OF THE DIMERIC CYTOCHROME BC1 COMPLEX FROM THE SOIL BACTERIUM PARACOCCUS DENITRIFICANS AT 2.7 ANGSTROM RESOLUTION

Structural highlights

2yiu is a 6 chain structure with sequence from Paracoccus denitrificans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Activity:	Ubiquinol--cytochrome-c reductase, with EC number 1.10.2.2
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CYB_PARDE] 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. [UCRI_PARDE] 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. [CY1_PARDE] 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.

Publication Abstract from PubMed

The respiratory cytochrome bc(1) complex is a fundamental enzyme in biological energy conversion. It couples electron transfer from ubiquinol to cytochrome c with generation of proton motive force which fuels ATP synthesis. The complex from the alpha-proteobacterium Paracoccus denitrificans, a model for the medically relevant mitochondrial complexes, lacked structural characterization. We show by LILBID mass spectrometry that truncation of the organism-specific, acidic N-terminus of cytochrome c(1) changes the oligomerization state of the enzyme to a dimer. The fully functional complex was crystallized and the X-ray structure determined at 2.7-A resolution. It has high structural homology to mitochondrial complexes and to the Rhodobacter sphaeroides complex especially for subunits cytochrome b and ISP. Species-specific binding of the inhibitor stigmatellin is noteworthy. Interestingly, cytochrome c(1) shows structural differences to the mitochondrial and even between the two Rhodobacteraceae complexes. The structural diversity in the cytochrome c(1) surface facing the ISP domain indicates low structural constraints on that surface for formation of a productive electron transfer complex. A similar position of the acidic N-terminal domains of cytochrome c(1) and yeast subunit QCR6p is suggested in support of a similar function. A model of the electron transfer complex with membrane-anchored cytochrome c(552), the natural substrate, shows that it can adopt the same orientation as the soluble substrate in the yeast complex. The full structural integrity of the P. denitrificans variant underpins previous mechanistic studies on intermonomer electron transfer and paves the way for using this model system to address open questions of structure/function relationships and inhibitor binding.

X-ray structure of the dimeric cytochrome bc(1) complex from the soil bacterium Paracoccus denitrificans at 2.7-A resolution.,Kleinschroth T, Castellani M, Trinh CH, Morgner N, Brutschy B, Ludwig B, Hunte C Biochim Biophys Acta. 2011 Oct 3. PMID:21996020^[1]

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

References

↑ Kleinschroth T, Castellani M, Trinh CH, Morgner N, Brutschy B, Ludwig B, Hunte C. X-ray structure of the dimeric cytochrome bc(1) complex from the soil bacterium Paracoccus denitrificans at 2.7-A resolution. Biochim Biophys Acta. 2011 Oct 3. PMID:21996020 doi:10.1016/j.bbabio.2011.09.017

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2yiu"

@@ Line 1: / Line 1: @@
 ==X-RAY STRUCTURE OF THE DIMERIC CYTOCHROME BC1 COMPLEX FROM THE SOIL BACTERIUM PARACOCCUS DENITRIFICANS AT 2.7 ANGSTROM RESOLUTION==
 <StructureSection load='2yiu' size='340' side='right' caption='[[2yiu]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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=SMA:STIGMATELLIN+A'>SMA</scene></td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquinol--cytochrome-c_reductase Ubiquinol--cytochrome-c reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.10.2.2 1.10.2.2] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2yiu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yiu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2yiu RCSB], [http://www.ebi.ac.uk/pdbsum/2yiu PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2yiu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yiu OCA], [http://pdbe.org/2yiu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2yiu RCSB], [http://www.ebi.ac.uk/pdbsum/2yiu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2yiu ProSAT]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/CYB_PARDE CYB_PARDE]] 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. [[http://www.uniprot.org/uniprot/UCRI_PARDE UCRI_PARDE]] 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. [[http://www.uniprot.org/uniprot/CY1_PARDE CY1_PARDE]] 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.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 15: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2yiu" style="background-color:#fffaf0;"></div>
 ==See Also==

2yiu

From Proteopedia

Revision as of 19:40, 11 August 2016

X-RAY STRUCTURE OF THE DIMERIC CYTOCHROME BC1 COMPLEX FROM THE SOIL BACTERIUM PARACOCCUS DENITRIFICANS AT 2.7 ANGSTROM RESOLUTION

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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