Projection structures of three photosynthetic complexes from Rhodobacter sphaeroides:: LH2 at 6 Å LH1 and RC-LH1 at 25 Å

被引:243
作者
Walz, T [1 ]
Jamieson, SJ [1 ]
Bowers, CM [1 ]
Bullough, PA [1 ]
Hunter, CN [1 ]
机构
[1] Univ Sheffield, Dept Mol Biol & Biotechnol, Krebs Inst Biomol Res, Sheffield S10 2TN, S Yorkshire, England
基金
英国惠康基金;
关键词
photosynthesis; electron crystallography; 2-D crystals; light-harvesting complexes; membrane protein;
D O I
10.1006/jmbi.1998.2050
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Three photosynthetic complexes, light-harvesting complex 2 (LH2), light-harvesting complex 1 (LH1), and the reaction centre-light-harvesting complex 1 photounit (RC-LH1), were purified from a single species of a purple bacterium, Rhodobacter sphaeroides, and reconstituted into two-dimensional (2-D) crystals. Vesicular 2-D crystals of LH1 and RC-LH1 were imaged in negative stain and projection maps at 25 Angstrom. resolution were produced. The rings formed by LH1 have approximately the same mean diameter as the LH1 rings from Rhodospirillum rubrum (similar to 90 Angstrom) and therefore are likely to be composed of 15 to 17 alpha beta subunits. In the projection map calculated from the RC-LH1 2-D crystals, the reaction centre is represented by an additional density in the centre of the ring formed by the LH1 subunits. The marked improvement of shape and fine structure after a rotational pre-alignment of the RC-LH1 unit cells before averaging strongly suggests that the RC is not in a unique orientation within the LH1 rings. Tubular crystals of LH2 showed a high degree of order and allowed calculation of a projection map at 6 Angstrom resolution from glucose-embedded specimens. The projection structure shows a ring of nine alpha beta subunits. Variation of the alpha-helical projection densities suggests that the 9-fold symmetry axis is tilted with respect to the membrane normal. (C) 1998 Academic Press.
引用
收藏
页码:833 / 845
页数:13
相关论文
共 47 条
[1]   STRUCTURE OF THE REACTION CENTER FROM RHODOBACTER-SPHAEROIDES R-26 - THE COFACTORS .1. [J].
ALLEN, JP ;
FEHER, G ;
YEATES, TO ;
KOMIYA, H ;
REES, DC .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1987, 84 (16) :5730-5734
[2]   3-DIMENSIONAL STRUCTURE DETERMINATION BY ELECTRON-MICROSCOPY OF TWO-DIMENSIONAL CRYSTALS [J].
AMOS, LA ;
HENDERSON, R ;
UNWIN, PNT .
PROGRESS IN BIOPHYSICS & MOLECULAR BIOLOGY, 1983, 39 (03) :183-231
[3]   ROLE OF THE PUFX PROTEIN IN PHOTOSYNTHETIC GROWTH OF RHODOBACTER-SPHAEROIDES .2. PUFX IS REQUIRED FOR EFFICIENT UBIQUINONE UBIQUINOL EXCHANGE BETWEEN THE REACTION-CENTER Q(B) SITE AND THE CYTOCHROME BC(1) COMPLEX [J].
BARZ, WP ;
VERMEGLIO, A ;
FRANCIA, F ;
VENTUROLI, G ;
MELANDRI, BA ;
OESTERHELT, D .
BIOCHEMISTRY, 1995, 34 (46) :15248-15258
[4]   ROLE OF PUFX PROTEIN IN PHOTOSYNTHETIC GROWTH OF RHODOBACTER-SPHAEROIDES .1. PUFX IS REQUIRED FOR EFFICIENT LIGHT-DRIVEN ELECTRON-TRANSFER AND PHOTOPHOSPHORYLATION UNDER ANAEROBIC CONDITIONS [J].
BARZ, WP ;
FRANCIA, F ;
VENTUROLI, G ;
MELANDRI, BA ;
VERMEGLIO, A ;
OESTERHELT, D .
BIOCHEMISTRY, 1995, 34 (46) :15235-15247
[5]   PHASE ACCURACY IN HIGH-RESOLUTION ELECTRON-MICROSCOPY OF TRIGONAL AND ORTHORHOMBIC PURPLE MEMBRANE [J].
BULLOUGH, PA ;
HENDERSON, R .
BIOPHYSICAL JOURNAL, 1990, 58 (03) :705-711
[6]   HIGH-RESOLUTION SPOT-SCAN ELECTRON-MICROSCOPY OF MICROCRYSTALS OF AN ALPHA-HELICAL COILED-COIL PROTEIN [J].
BULLOUGH, PA ;
TULLOCH, PA .
JOURNAL OF MOLECULAR BIOLOGY, 1990, 215 (01) :161-173
[7]   STRUCTURE OF RHODOPSEUDOMONAS-SPHAEROIDES R-26 REACTION CENTER [J].
CHANG, CH ;
TIEDE, D ;
TANG, J ;
SMITH, U ;
NORRIS, J ;
SCHIFFER, M .
FEBS LETTERS, 1986, 205 (01) :82-86
[8]   The purple bacterial photosynthetic unit [J].
Cogdell, RJ ;
Fyfe, PK ;
Barrett, SJ ;
Prince, SM ;
Freer, AA ;
Isaacs, NW ;
McGlynn, P ;
Hunter, CN .
PHOTOSYNTHESIS RESEARCH, 1996, 48 (1-2) :55-63
[9]   MRC image processing programs [J].
Crowther, RA ;
Henderson, R ;
Smith, JM .
JOURNAL OF STRUCTURAL BIOLOGY, 1996, 116 (01) :9-16
[10]   STRUCTURE OF THE PROTEIN SUBUNITS IN THE PHOTOSYNTHETIC REACTION CENTER OF RHODOPSEUDOMONAS-VIRIDIS AT 3A RESOLUTION [J].
DEISENHOFER, J ;
EPP, O ;
MIKI, K ;
HUBER, R ;
MICHEL, H .
NATURE, 1985, 318 (6047) :618-624