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PDBsum entry 1prc

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Photosynthetic reaction center PDB id
1prc
Contents
Protein chains
333 a.a. *
273 a.a. *
323 a.a. *
258 a.a. *
Ligands
HEC ×4
BCB ×4
BPB ×2
UQ1
SO4 ×7
MQ7
NS1
LDA ×2
Metals
_FE
Waters ×201
* Residue conservation analysis

References listed in PDB file
Key reference
Title Crystallographic refinement at 2.3 a resolution and refined model of the photosynthetic reaction centre from rhodopseudomonas viridis.
Authors J.Deisenhofer, O.Epp, I.Sinning, H.Michel.
Ref. J Mol Biol, 1995, 246, 429-457.
PubMed id 7877166
Note In the PDB file this reference is annotated as "TO BE PUBLISHED". The citation details given above were identified by an automated search of PubMed on title and author names, giving a percentage match of 95%.
Abstract
The atomic model of the photosynthetic reaction centre from the purple bacterium Rhodopseudomonas viridis has been refined to an R-value of 0.193 at 2.3 A resolution. The refined model contains 10,288 non-hydrogen atoms; 10,045 of these have well defined electron density. A Luzzati-plot indicates an average co-ordinate error of 0.26 A. During refinement, the positions of a partially ordered carotenoid, a unibiquinone in the partially occupied QB site, a detergent molecule, seven putative sulphate ions, and 201 water molecules were found. More than half of these waters are bound at interfaces between protein subunits and therefore contribute significantly to subunit interactions. Water molecules also play important structural and probably functional roles in the environment of some of the cofactors. Two water molecules form hydrogen bonds to the accessory bacteriochlorophylls and to the protein in the vicinity of the special pair of bacteriophylls, the primary electron donor. A group of about 10 water molecules is bound near the binding site of the secondary quinone QB. These waters are likely to participate in the transfer of protons to the doubly reduced QB.
Secondary reference #1
Title The photosynthetic reaction center from the purple bacterium rhodopseudomonas viridis.
Authors J.Deisenhofer, H.Michel.
Ref. Science, 1989, 245, 1463-1473.
PubMed id 17776797
Abstract
Secondary reference #2
Title Structure of the protein subunits in the photosynthetic reaction centre of rhodopseudomonas viridis at 3 angstroms resolution
Authors J.Deisenhofer, O.Epp, K.Miki, R.Huber, H.Michel.
Ref. nature, 1985, 318, 618.
Secondary reference #3
Title X-Ray structure analysis of a membrane protein complex. Electron density map at 3 a resolution and a model of the chromophores of the photosynthetic reaction center from rhodopseudomonas viridis.
Authors J.Deisenhofer, O.Epp, K.Miki, R.Huber, H.Michel.
Ref. J Mol Biol, 1984, 180, 385-398. [DOI no: 10.1016/S0022-2836(84)80011-X]
PubMed id 6392571
Full text Abstract
Figure 3.
Fro. 3. Stereo draing of the special pair. The central local symmetry ais runs between the BChl-bs. Ring numbers are indicated in one BChl-b. Phytyl chains are truncated.
Figure 4.
FIG. 4. Stereo drawing of the prosthetic grups of the RC shwing 4 BChl-b (BC), 2 BPh-b (BP), 1 non-eine iron (Fe), 1 quinone (MQ) an heine grups (HE). The central local symmetry axis runs vertically in the plane of the picture. The plane of the membane is assumed t be oriented perpendicular to the central local symmetry axis, i.e. horizontal and perpendicular to the plane of th picture. The dotted lines marked 0 and I indicate the presmed approximate outer and inner membrane surfaces of the bacterial cell. The BChl-b, BPh-b, quinone and iron are lcated within th cylindrical central part of the RC compex; te ~ 70 A diameter of the cylinder is perpendicular to th local symmetry axis in the plane of the picture
The above figures are reproduced from the cited reference with permission from Elsevier
Secondary reference #4
Title Three-Dimensional crystals of a membrane protein complex. The photosynthetic reaction centre from rhodopseudomonas viridis.
Author H.Michel.
Ref. J Mol Biol, 1982, 158, 567-572. [DOI no: 10.1016/0022-2836(82)90216-9]
PubMed id 7131557
Full text Abstract
Figure 1.
IG:. 1. Elation profile of the molecular siev chromatograph step used for the isolation of thr photosvnthetic reaction centrrs from tl. Gridis. I'hotosynthrtir membranes (I6 mg of protein/ml) were solubil&d in 5''' f. w/v) S.K~dod~c?ildimet,h~lamine A-oxide. WI O,> (y/v) Sx3. 10 mwTris_ HCI (pH 7) at room temprratre for 5 mill. After a clarifying spin (1OO,OOOg, 30 min). 09.5 ml of the supwnatant was applird to a. TSK 3ooO SW column (LKH. (ZrLfelfing) and run nt 0.1 ml/in in 20 mM-sodium phosphat,r (pH 7). 0.1 `)o (w/r) S,S-dodervldimc,th?aminr A-oxide, PI'',, (W/V) NaN,. The reaction crntres form the prak arktad I%(`.
The above figure is reproduced from the cited reference with permission from Elsevier
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