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PDBsum entry 1kb9
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protein ligands Protein-protein interface(s) links
Oxidoreductase/electron transport PDB id
1kb9

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
431 a.a. *
352 a.a. *
385 a.a. *
246 a.a. *
185 a.a. *
74 a.a. *
125 a.a. *
93 a.a. *
55 a.a. *
127 a.a. *
107 a.a. *
Ligands
PCF
UMQ
HEM ×3
SMA
UQ6
PIE
PEF ×2
CDL
FES
Waters ×321
* Residue conservation analysis
PDB id:
1kb9
Name: Oxidoreductase/electron transport
Title: Yeast cytochrome bc1 complex
Structure: Ubiquinol-cytochromE C reductase complex core protein i. Chain: a. Fragment: residues 27-457. Engineered: yes. Ubiquinol-cytochromE C reductase complex core protein 2. Chain: b. Fragment: residues 17-368. Engineered: yes. Cytochrome b.
Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Organelle: mitochondria. Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: 22mer (from PQS)
Resolution:
2.30Å     R-factor:   0.218     R-free:   0.249
Authors: C.Lange,J.H.Nett,B.L.Trumpower,C.Hunte
Key ref:
C.Lange et al. (2001). Specific roles of protein-phospholipid interactions in the yeast cytochrome bc1 complex structure. EMBO J, 20, 6591-6600. PubMed id: 11726495 DOI: 10.1093/emboj/20.23.6591
Date:
05-Nov-01     Release date:   18-Sep-02    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P07256  (QCR1_YEAST) -  Cytochrome b-c1 complex subunit 1, mitochondrial from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc: 		457 a.a.
431 a.a.*
Protein chain
Pfam   ArchSchema ?
P07257  (QCR2_YEAST) -  Cytochrome b-c1 complex subunit 2, mitochondrial from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc: 		368 a.a.
352 a.a.
Protein chain
Pfam   ArchSchema ?
P00163  (CYB_YEAST) -  Cytochrome b from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc: 		385 a.a.
385 a.a.*
Protein chain
Pfam   ArchSchema ?
P07143  (CY1_YEAST) -  Cytochrome c1, heme protein, mitochondrial from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc: 		309 a.a.
246 a.a.
Protein chain
Pfam   ArchSchema ?
P08067  (UCRI_YEAST) -  Cytochrome b-c1 complex subunit Rieske, mitochondrial from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc: 		215 a.a.
185 a.a.
Protein chain
Pfam   ArchSchema ?
P00127  (QCR6_YEAST) -  Cytochrome b-c1 complex subunit 6, mitochondrial from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc: 		147 a.a.
74 a.a.
Protein chain
Pfam   ArchSchema ?
P00128  (QCR7_YEAST) -  Cytochrome b-c1 complex subunit 7, mitochondrial from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc: 		127 a.a.
125 a.a.
Protein chain
Pfam   ArchSchema ?
P08525  (QCR8_YEAST) -  Cytochrome b-c1 complex subunit 8, mitochondrial from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc: 		94 a.a.
93 a.a.
Protein chain
Pfam   ArchSchema ?
P22289  (QCR9_YEAST) -  Cytochrome b-c1 complex subunit 9, mitochondrial from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc: 		66 a.a.
55 a.a.
Protein chain
No UniProt id for this chain
Struc: 127 a.a.
Protein chain
No UniProt id for this chain
Struc: 107 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class 2: Chains A, B, F, G, H, I: E.C.1.10.2.2  - Transferred entry: 7.1.1.8.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+
Quinol
 + 2 × ferricytochrome c
 = quinone
 + 2 × ferrocytochrome c
 + 2 × H(+)
   Enzyme class 3: Chains C, D, E: E.C.7.1.1.8  - quinol--cytochrome-c reductase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2 Fe(II)- [cytochrome c](out) + 2 H(+)(out)
quinol
 + 2 × Fe(III)-[cytochrome c](out)
 = quinone
 + 2 × Fe(II)- [cytochrome c](out)
 + 2 × H(+)(out)
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1093/emboj/20.23.6591 EMBO J 20:6591-6600 (2001)
PubMed id: 11726495  
 
 
Specific roles of protein-phospholipid interactions in the yeast cytochrome bc1 complex structure.
C.Lange, J.H.Nett, B.L.Trumpower, C.Hunte.
 
  ABSTRACT  
 
Biochemical data have shown that specific, tightly bound phospholipids are essential for activity of the cytochrome bc1 complex (QCR), an integral membrane protein of the respiratory chain. However, the structure and function of such phospholipids are not yet known. Here we describe five phospholipid molecules and one detergent molecule in the X-ray structure of yeast QCR at 2.3 A resolution. Their individual binding sites suggest specific roles in facilitating structural and functional integrity of the enzyme. Interestingly, a phosphatidylinositol molecule is bound in an unusual interhelical position near the flexible linker region of the Rieske iron-sulfur protein. Two possible proton uptake pathways at the ubiquinone reduction site have been identified: the E/R and the CL/K pathway. Remarkably, cardiolipin is positioned at the entrance to the latter. We propose that cardiolipin ensures structural integrity of the proton-conducting protein environment and takes part directly in proton uptake. Site-directed mutagenesis of ligating residues confirmed the importance of the phosphatidylinositol- and cardiolipin-binding sites.
 
  Selected figure(s)  
 
Figure 5.
Figure 5 Section of the yeast QCR model showing L5 (cardiolipin), neighboring amino acid residues and water molecules. Hydrogen bonds or ion pairs with the oxygen atoms of the phosphodiester groups A and B of the cardiolipin headgroup are indicated as dashed lines (Lys288, Lys289 of CYT1, Tyr28 of COB). Water molecules are shown as balls, and other molecules in stick presentation. The final 2F[o] - F[c] electron density map (blue -gray) is contoured at 1.0 . Atoms are shown in standard colors. 		Figure 7.
Figure 7 Putative proton uptake pathways at the Q[i] site of yeast QCR via two arrays of hydrogen-bonded water molecules, which connect the bulk solvent at the matrix side with the site of ubiquinone reduction. The entrance to the E/R pathway is formed by Glu52 of QCR7 and Wat176. The gating residue towards the quinone-binding pocket is Arg218 of COB. Cardiolipin (L5) is positioned at the entrance to the CL/K pathway, for which Lys228 of COB is the gating residue. Arrows indicate the access sites from the bulk solvent, and double arrows show proton transfer between the key residues Arg218 or Lys228 of COB and UQ6. Side chains of amino acid residues that are involved in hydrogen bond interactions or ion pair formation are shown (standard colors). Dashed lines indicate hydrogen bond interactions. Dotted lines are used for hydrogen bond interactions of UQ6 and CL ligands (His202, Asp229 and Tyr28 of COB, and Lys288 and Lys289 of CYT1). Water molecules in the cavity above the cardiolipin headgroup are stabilized by interactions with side chains of Lys228 of COB, Lys296 of CYT1 and His85 of QCR7. A surrounding layer of non-polar residues (not shown) encloses the water-filled cavity. Transmembrane helices are shown as ribbon presentation and other polypeptide backbones as rope presentation. UQ6, heme b[H] and CL are represented as stick models.
 
  The above figures are reprinted from an Open Access publication published by Macmillan Publishers Ltd: EMBO J (2001, 20, 6591-6600) copyright 2001.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21220505 C.Osman, D.R.Voelker, and T.Langer (2011).
Making heads or tails of phospholipids in mitochondria.
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21518899 R.Arias-Cartin, S.Grimaldi, J.Pommier, P.Lanciano, C.Schaefer, P.Arnoux, G.Giordano, B.Guigliarelli, and A.Magalon (2011).
Cardiolipin-based respiratory complex activation in bacteria.
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20657548 C.Potting, C.Wilmes, T.Engmann, C.Osman, and T.Langer (2010).
Regulation of mitochondrial phospholipids by Ups1/PRELI-like proteins depends on proteolysis and Mdm35.
  EMBO J, 29, 2888-2898.  
19739941 G.Lenaz, and M.L.Genova (2010).
Structure and organization of mitochondrial respiratory complexes: a new understanding of an old subject.
  Antioxid Redox Signal, 12, 961.  
21081696 G.Z.Wu, and H.W.Xue (2010).
Arabidopsis β-ketoacyl-[acyl carrier protein] synthase i is crucial for fatty acid synthesis and plays a role in chloroplast division and embryo development.
  Plant Cell, 22, 3726-3744.  
20544074 J.Gubbens, and A.I.de Kroon (2010).
Proteome-wide detection of phospholipid-protein interactions in mitochondria by photocrosslinking and click chemistry.
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20095951 J.Van Galen, B.W.Van Balkom, R.L.Serrano, D.Kaloyanova, R.Eerland, E.Stüven, and J.B.Helms (2010).
Binding of GAPR-1 to negatively charged phospholipid membranes: unusual binding characteristics to phosphatidylinositol.
  Mol Membr Biol, 27, 81-91.  
20139086 M.F.Lensink, C.Govaerts, and J.M.Ruysschaert (2010).
Identification of specific lipid-binding sites in integral membrane proteins.
  J Biol Chem, 285, 10519-10526.  
20352202 M.Raja (2010).
The role of phosphatidic acid and cardiolipin in stability of the tetrameric assembly of potassium channel KcsA.
  J Membr Biol, 234, 235-240.  
19224349 C.Cortés-Rojo, E.Calderón-Cortés, M.Clemente-Guerrero, M.Estrada-Villagómez, S.Manzo-Avalos, R.Mejía-Zepeda, I.Boldogh, and A.Saavedra-Molina (2009).
Elucidation of the effects of lipoperoxidation on the mitochondrial electron transport chain using yeast mitochondria with manipulated fatty acid content.
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19371718 E.Mileykovskaya, and W.Dowhan (2009).
Cardiolipin membrane domains in prokaryotes and eukaryotes.
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19711505 G.Lenaz, and M.L.Genova (2009).
Structural and functional organization of the mitochondrial respiratory chain: a dynamic super-assembly.
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19165886 I.Schuiki, and G.Daum (2009).
Phosphatidylserine decarboxylases, key enzymes of lipid metabolism.
  IUBMB Life, 61, 151-162.  
19413994 M.Schlame, and M.Ren (2009).
The role of cardiolipin in the structural organization of mitochondrial membranes.
  Biochim Biophys Acta, 1788, 2080-2083.  
19175316 R.E.Berry, M.N.Shokhirev, A.Y.Ho, F.Yang, T.K.Shokhireva, H.Zhang, A.Weichsel, W.R.Montfort, and F.A.Walker (2009).
Effect of mutation of carboxyl side-chain amino acids near the heme on the midpoint potentials and ligand binding constants of nitrophorin 2 and its NO, histamine, and imidazole complexes.
  J Am Chem Soc, 131, 2313-2327.
PDB code: 3fll
19422785 S.M.Claypool (2009).
Cardiolipin, a critical determinant of mitochondrial carrier protein assembly and function.
  Biochim Biophys Acta, 1788, 2059-2068.  
19503808 W.A.Beckstead, M.T.Ebbert, M.J.Rowe, and D.A.McClellan (2009).
Evolutionary pressure on mitochondrial cytochrome b is consistent with a role of CytbI7T affecting longevity during caloric restriction.
  PLoS One, 4, e5836.  
18418633 E.A.Berry, and F.A.Walker (2008).
Bis-histidine-coordinated hemes in four-helix bundles: how the geometry of the bundle controls the axial imidazole plane orientations in transmembrane cytochromes of mitochondrial complexes II and III and related proteins.
  J Biol Inorg Chem, 13, 481-498.  
18719951 E.N.Brown, R.Friemann, A.Karlsson, J.V.Parales, M.M.Couture, L.D.Eltis, and S.Ramaswamy (2008).
Determining Rieske cluster reduction potentials.
  J Biol Inorg Chem, 13, 1301-1313.
PDB code: 2qpz
18759116 E.Tichá, V.Polakovicová, and M.Obernauerová (2008).
Regulation of phosphatidylglycerolphosphate synthase in aerobic yeast Kluyveromyces lactis.
  Folia Microbiol (Praha), 53, 319-324.  
18606003 J.Chen, H.Liang, and A.Fernández (2008).
Protein structure protection commits gene expression patterns.
  Genome Biol, 9, R107.  
17922302 J.N.Sturgis, and R.A.Niederman (2008).
Atomic force microscopy reveals multiple patterns of antenna organization in purple bacteria: implications for energy transduction mechanisms and membrane modeling.
  Photosynth Res, 95, 269-278.  
18039651 L.Esser, M.Elberry, F.Zhou, C.A.Yu, L.Yu, and D.Xia (2008).
Inhibitor-complexed Structures of the Cytochrome bc1 from the Photosynthetic Bacterium Rhodobacter sphaeroides.
  J Biol Chem, 283, 2846-2857.
PDB codes: 2qjk 2qjp 2qjy
  18751913 M.Bogdanov, E.Mileykovskaya, and W.Dowhan (2008).
Lipids in the assembly of membrane proteins and organization of protein supercomplexes: implications for lipid-linked disorders.
  Subcell Biochem, 49, 197-239.  
18077827 M.Schlame (2008).
Cardiolipin synthesis for the assembly of bacterial and mitochondrial membranes.
  J Lipid Res, 49, 1607-1620.  
18234676 P.Hakizimana, M.Masureel, B.Gbaguidi, J.M.Ruysschaert, and C.Govaerts (2008).
Interactions between phosphatidylethanolamine headgroup and LmrP, a multidrug transporter: a conserved mechanism for proton gradient sensing?
  J Biol Chem, 283, 9369-9376.  
18180306 S.L.Cuddihy, S.S.Ali, E.S.Musiek, J.Lucero, S.J.Kopp, J.D.Morrow, and L.L.Dugan (2008).
Prolonged alpha-tocopherol deficiency decreases oxidative stress and unmasks alpha-tocopherol-dependent regulation of mitochondrial function in the brain.
  J Biol Chem, 283, 6915-6924.  
17457691 D.Xia, L.Esser, L.Yu, and C.A.Yu (2007).
Structural basis for the mechanism of electron bifurcation at the quinol oxidation site of the cytochrome bc1 complex.
  Photosynth Res, 92, 17-34.  
17873079 I.Marques, N.A.Dencher, A.Videira, and F.Krause (2007).
Supramolecular organization of the respiratory chain in Neurospora crassa mitochondria.
  Eukaryot Cell, 6, 2391-2405.  
17332748 K.Shinzawa-Itoh, H.Aoyama, K.Muramoto, H.Terada, T.Kurauchi, Y.Tadehara, A.Yamasaki, T.Sugimura, S.Kurono, K.Tsujimoto, T.Mizushima, E.Yamashita, T.Tsukihara, and S.Yoshikawa (2007).
Structures and physiological roles of 13 integral lipids of bovine heart cytochrome c oxidase.
  EMBO J, 26, 1713-1725.
PDB codes: 2dyr 2dys
16963124 M.R.Jones (2007).
Lipids in photosynthetic reaction centres: structural roles and functional holes.
  Prog Lipid Res, 46, 56-87.  
17293402 R.N.Lewis, D.Zweytick, G.Pabst, K.Lohner, and R.N.McElhaney (2007).
Calorimetric, x-ray diffraction, and spectroscopic studies of the thermotropic phase behavior and organization of tetramyristoyl cardiolipin membranes.
  Biophys J, 92, 3166-3177.  
17616531 S.A.Dikanov, J.T.Holland, B.Endeward, D.R.Kolling, R.I.Samoilova, T.F.Prisner, and A.R.Crofts (2007).
Hydrogen bonds between nitrogen donors and the semiquinone in the Qi-site of the bc1 complex.
  J Biol Chem, 282, 25831-25841.  
17680760 V.I.Kulinsky, and L.S.Kolesnichenko (2007).
Mitochondrial glutathione.
  Biochemistry (Mosc), 72, 698-701.  
17534481 X.Liang, D.J.Campopiano, and P.J.Sadler (2007).
Metals in membranes.
  Chem Soc Rev, 36, 968-992.  
16586113 F.A.Walker (2006).
The heme environment of mouse neuroglobin: histidine imidazole plane orientations obtained from solution NMR and EPR spectroscopy as compared with X-ray crystallography.
  J Biol Inorg Chem, 11, 391-397.  
16934675 L.Huang, D.Tang, M.C.Yappert, and D.Borchman (2006).
Oxidation-induced changes in human lens epithelial cells 2. Mitochondria and the generation of reactive oxygen species.
  Free Radic Biol Med, 41, 926-936.  
16358245 R.Hielscher, T.Wenz, S.Stolpe, C.Hunte, T.Friedrich, and P.Hellwig (2006).
Monitoring redox-dependent contribution of lipids in Fourier transform infrared difference spectra of complex I from Escherichia coli.
  Biopolymers, 82, 291-294.  
16856942 S.Aygun-Sunar, S.Mandaci, H.G.Koch, I.V.Murray, H.Goldfine, and F.Daldal (2006).
Ornithine lipid is required for optimal steady-state amounts of c-type cytochromes in Rhodobacter capsulatus.
  Mol Microbiol, 61, 418-435.  
16433558 T.Teschner, L.Yatsunyk, V.Schünemann, H.Paulsen, H.Winkler, C.Hu, W.R.Scheidt, F.A.Walker, and A.X.Trautwein (2006).
Models of the membrane-bound cytochromes: mössbauer spectra of crystalline low-spin ferriheme complexes having axial ligand plane dihedral angles ranging from 0 degree to 90 degrees.
  J Am Chem Soc, 128, 1379-1389.  
16544270 X.Su, and W.Dowhan (2006).
Regulation of cardiolipin synthase levels in Saccharomyces cerevisiae.
  Yeast, 23, 279-291.  
16880984 A.G.Lee (2005).
How lipids and proteins interact in a membrane: a molecular approach.
  Mol Biosyst, 1, 203-212.  
16172928 A.J.Watson, A.V.Hughes, P.K.Fyfe, M.C.Wakeham, K.Holden-Dye, P.Heathcote, and M.R.Jones (2005).
On the role of basic residues in adapting the reaction centre-LH1 complex for growth at elevated temperatures in purple bacteria.
  Photosynth Res, 86, 81.  
16355230 B.Loll, J.Kern, W.Saenger, A.Zouni, and J.Biesiadka (2005).
Towards complete cofactor arrangement in the 3.0 A resolution structure of photosystem II.
  Nature, 438, 1040-1044.
PDB code: 2axt
15807653 E.Mileykovskaya, M.Zhang, and W.Dowhan (2005).
Cardiolipin in energy transducing membranes.
  Biochemistry (Mosc), 70, 154-158.  
16211522 H.Zhang, and W.A.Cramer (2005).
Problems in obtaining diffraction-quality crystals of hetero-oligomeric integral membrane proteins.
  J Struct Funct Genomics, 6, 219-223.  
16150713 K.Obara, N.Miyashita, C.Xu, I.Toyoshima, Y.Sugita, G.Inesi, and C.Toyoshima (2005).
Structural role of countertransport revealed in Ca(2+) pump crystal structure in the absence of Ca(2+).
  Proc Natl Acad Sci U S A, 102, 14489-14496.
PDB code: 2agv
  16873926 M.L.Genova, C.Bianchi, and G.Lenaz (2005).
Supercomplex organization of the mitochondrial respiratory chain and the role of the Coenzyme Q pool: pathophysiological implications.
  Biofactors, 25, 5.  
15972817 M.Zhang, E.Mileykovskaya, and W.Dowhan (2005).
Cardiolipin is essential for organization of complexes III and IV into a supercomplex in intact yeast mitochondria.
  J Biol Chem, 280, 29403-29408.  
15949761 P.K.Fyfe, A.V.Hughes, P.Heathcote, and M.R.Jones (2005).
Proteins, chlorophylls and lipids: X-ray analysis of a three-way relationship.
  Trends Plant Sci, 10, 275-282.  
16298733 T.Koumura, C.Nakamura, and Y.Nakagawa (2005).
Role of calcium-induced mitochondrial hydroperoxide in induction of apoptosis of RBL2H3 cells with eicosapentaenoic acid treatment.
  Free Radic Res, 39, 1083-1089.  
15759116 Z.Kronekova, and G.Rödel (2005).
Organization of assembly factors Cbp3p and Cbp4p and their effect on bc(1) complex assembly in Saccharomyces cerevisiae.
  Curr Genet, 47, 203-212.  
14977419 A.R.Crofts (2004).
The cytochrome bc1 complex: function in the context of structure.
  Annu Rev Physiol, 66, 689-733.  
15044453 F.Krause, C.Q.Scheckhuber, A.Werner, S.Rexroth, N.H.Reifschneider, N.A.Dencher, and H.D.Osiewacz (2004).
Supramolecular organization of cytochrome c oxidase- and alternative oxidase-dependent respiratory chains in the filamentous fungus Podospora anserina.
  J Biol Chem, 279, 26453-26461.  
15475362 G.Petrosillo, F.M.Ruggiero, M.Pistolese, and G.Paradies (2004).
Ca2+-induced reactive oxygen species production promotes cytochrome c release from rat liver mitochondria via mitochondrial permeability transition (MPT)-dependent and MPT-independent mechanisms: role of cardiolipin.
  J Biol Chem, 279, 53103-53108.  
15465855 S.S.Deol, P.J.Bond, C.Domene, and M.S.Sansom (2004).
Lipid-protein interactions of integral membrane proteins: a comparative simulation study.
  Biophys J, 87, 3737-3749.  
15273291 S.Scheuring, J.N.Sturgis, V.Prima, A.Bernadac, D.Lévy, and J.L.Rigaud (2004).
Watching the photosynthetic apparatus in native membranes.
  Proc Natl Acad Sci U S A, 101, 11293-11297.  
15044463 U.Schlattner, F.Gehring, N.Vernoux, M.Tokarska-Schlattner, D.Neumann, O.Marcillat, C.Vial, and T.Wallimann (2004).
C-terminal lysines determine phospholipid interaction of sarcomeric mitochondrial creatine kinase.
  J Biol Chem, 279, 24334-24342.  
15292198 V.M.Gohil, P.Hayes, S.Matsuyama, H.Schägger, M.Schlame, and M.L.Greenberg (2004).
Cardiolipin biosynthesis and mitochondrial respiratory chain function are interdependent.
  J Biol Chem, 279, 42612-42618.  
15126295 Y.Nakagawa (2004).
Initiation of apoptotic signal by the peroxidation of cardiolipin of mitochondria.
  Ann N Y Acad Sci, 1011, 177-184.  
14640699 A.M.Powl, J.M.East, and A.G.Lee (2003).
Lipid-protein interactions studied by introduction of a tryptophan residue: the mechanosensitive channel MscL.
  Biochemistry, 42, 14306-14317.  
14647374 D.Stroebel, Y.Choquet, J.L.Popot, and D.Picot (2003).
An atypical haem in the cytochrome b(6)f complex.
  Nature, 426, 413-418.
PDB code: 1q90
12521597 H.Imai, and Y.Nakagawa (2003).
Biological significance of phospholipid hydroperoxide glutathione peroxidase (PHGPx, GPx4) in mammalian cells.
  Free Radic Biol Med, 34, 145-169.  
12782631 H.Palsdottir, C.G.Lojero, B.L.Trumpower, and C.Hunte (2003).
Structure of the yeast cytochrome bc1 complex with a hydroxyquinone anion Qo site inhibitor bound.
  J Biol Chem, 278, 31303-31311.
PDB code: 1p84
12702760 H.Zhang, G.Kurisu, J.L.Smith, and W.A.Cramer (2003).
A defined protein-detergent-lipid complex for crystallization of integral membrane proteins: The cytochrome b6f complex of oxygenic photosynthesis.
  Proc Natl Acad Sci U S A, 100, 5160-5163.  
14561769 K.Pfeiffer, V.Gohil, R.A.Stuart, C.Hunte, U.Brandt, M.L.Greenberg, and H.Schägger (2003).
Cardiolipin stabilizes respiratory chain supercomplexes.
  J Biol Chem, 278, 52873-52880.  
14645072 S.J.Alvis, I.M.Williamson, J.M.East, and A.G.Lee (2003).
Interactions of anionic phospholipids and phosphatidylethanolamine with the potassium channel KcsA.
  Biophys J, 85, 3828-3838.  
14551214 Y.Xu, R.I.Kelley, T.J.Blanck, and M.Schlame (2003).
Remodeling of cardiolipin by phospholipid transacylation.
  J Biol Chem, 278, 51380-51385.  
12163074 C.Hunte, and H.Michel (2002).
Crystallisation of membrane proteins mediated by antibody fragments.
  Curr Opin Struct Biol, 12, 503-508.  
12364341 M.Zhang, E.Mileykovskaya, and W.Dowhan (2002).
Gluing the respiratory chain together. Cardiolipin is required for supercomplex formation in the inner mitochondrial membrane.
  J Biol Chem, 277, 43553-43556.  
12475926 V.Helms (2002).
Attraction within the membrane. Forces behind transmembrane protein folding and supramolecular complex assembly.
  EMBO Rep, 3, 1133-1138.  
12384503 Y.Saint-Georges, N.Bonnefoy, J.P.di Rago, S.Chiron, and G.Dujardin (2002).
A pathogenic cytochrome b mutation reveals new interactions between subunits of the mitochondrial bc1 complex.
  J Biol Chem, 277, 49397-49402.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.

 

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