Structure of monomeric yeast and mammalian Sec61 complexes interacting with the translating ribosome

Science

Volumn 326, Issue 5958, 2009, Pages 1369-1373

  Becker, Thomas ^a   Bhushan, Shashi ^a   Jarasch, Alexander ^a   Armache, Jean Paul ^a   Funes, Soledad ^a,b   Jossinet, Fabrice ^c   Gumbart, James ^d   Mielke, Thorsten ^e,f   Berninghausen, Otto ^a   Schulten, Klaus ^d   Westhof, Eric ^c   Gilmore, Reid ^g   Mandon, Elisabet C ^g   Beckmann, Roland ^a  

^a UNIVERSITY OF MUNICH   (Germany)

^b UNIVERSIDAD NACIONAL AUTÓNOMA DE MÉXICO   (Mexico)

^c UNIVERSITÉ DE STRASBOURG   (France)

^d UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

^e MAX PLANCK INSTITUTE FOR MOLECULAR GENETICS   (Germany)

^f CHARITÉ UNIVERSITÄTSMEDIZIN BERLIN   (Germany)

^g UNIVERSITY OF MASSACHUSETTS MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; OLIGOMER; SEC61 PROTEIN; SECRETORY PROTEIN; UNCLASSIFIED DRUG;

BIOCHEMICAL COMPOSITION; CYTOPLASM; DATA SET; ELECTRON MICROSCOPY; EUKARYOTE; PROTEIN; RNA; YEAST;

ARTICLE; CHEMICAL ANALYSIS; COMPLEX FORMATION; CRYOELECTRON MICROSCOPY; CYTOPLASM; ENZYME ACTIVE SITE; EUKARYOTE; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTEIN TRANSPORT; RIBOSOME; SACCHAROMYCES CEREVISIAE; THREE DIMENSIONAL IMAGING; YEAST;

ANIMALS; BINDING SITES; CRYOELECTRON MICROSCOPY; DOGS; IMAGE PROCESSING, COMPUTER-ASSISTED; MEMBRANE PROTEINS; MODELS, MOLECULAR; PROTEIN BIOSYNTHESIS; PROTEIN CONFORMATION; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN TRANSPORT; PROTEINS; RIBOSOMES; SACCHAROMYCES CEREVISIAE PROTEINS;

EUKARYOTA; MAMMALIA;

EID: 71549167617     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1178535     Document Type: Article

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40. We thank B. Dobberstein (Zentrum für Molekulare Biologie der Universität Heidelberg, Heidelberg, Germany) for microsomal membranes, B, Brügger (Biochemie-Zentrum der Universität Heidelberg, Heidelberg, Germany) for lipid analysis, and J. Frauenfeld and E. van der Sluis for critical discussions. This research was supported by Deutsche Forschungsgemeinschaft grants SFB594, SFB646 (to R.B. and T.B.), and SFB 740 (to T.M.); Knut and Alice Wallenberg Foundation, Stockholm, Sweden (to S.B.); NIH grants P41-RR05969, R01-GM067887 (to K.S.), and GM35687 (to R.G.); NSF grant PHY0822613 (to K.S.); and the European Union and Senatsverwaltung für Wissenschaft, Forschung und Kultur Berlin (UltraStructureNetwork, Anwenderzentrum). Computer time for MDFF was provided through an NSF Large Resources Allocation Committee grant (MCA93S028). Coordinates of the atomic models and cryo-EM maps have been deposited in the PDB [with accession numbers 2ww9 (active Ssh), 2wwa (inactive Ssh), and 2wwb (mammalian translocon)] and in the 3D-EM database [EMD-1651 (yeast) and EMD-1652 (Mammalia)], respectively.