4rcr

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[[Image:4rcr.jpg|left|200px]]<br /><applet load="4rcr" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:4rcr.jpg|left|200px]]
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caption="4rcr, resolution 2.8&Aring;" />
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'''STRUCTURE OF THE REACTION CENTER FROM RHODOBACTER SPHAEROIDES R-26 AND 2.4.1: PROTEIN-COFACTOR (BACTERIOCHLOROPHYLL, BACTERIOPHEOPHYTIN, AND CAROTENOID) INTERACTIONS'''<br />
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{{Structure
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|PDB= 4rcr |SIZE=350|CAPTION= <scene name='initialview01'>4rcr</scene>, resolution 2.8&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=BCL:BACTERIOCHLOROPHYLL+A'>BCL</scene>, <scene name='pdbligand=BPH:BACTERIOPHEOPHYTIN+A'>BPH</scene> and <scene name='pdbligand=U10:UBIQUINONE-10'>U10</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''STRUCTURE OF THE REACTION CENTER FROM RHODOBACTER SPHAEROIDES R-26 AND 2.4.1: PROTEIN-COFACTOR (BACTERIOCHLOROPHYLL, BACTERIOPHEOPHYTIN, AND CAROTENOID) INTERACTIONS'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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4RCR is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides] with <scene name='pdbligand=BOG:'>BOG</scene>, <scene name='pdbligand=FE:'>FE</scene>, <scene name='pdbligand=BCL:'>BCL</scene>, <scene name='pdbligand=BPH:'>BPH</scene> and <scene name='pdbligand=U10:'>U10</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RCR OCA].
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4RCR is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RCR OCA].
==Reference==
==Reference==
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Structure of the reaction center from Rhodobacter sphaeroides R-26 and 2.4.1: protein-cofactor (bacteriochlorophyll, bacteriopheophytin, and carotenoid) interactions., Yeates TO, Komiya H, Chirino A, Rees DC, Allen JP, Feher G, Proc Natl Acad Sci U S A. 1988 Nov;85(21):7993-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=3186702 3186702]
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Structure of the reaction center from Rhodobacter sphaeroides R-26 and 2.4.1: protein-cofactor (bacteriochlorophyll, bacteriopheophytin, and carotenoid) interactions., Yeates TO, Komiya H, Chirino A, Rees DC, Allen JP, Feher G, Proc Natl Acad Sci U S A. 1988 Nov;85(21):7993-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/3186702 3186702]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Rhodobacter sphaeroides]]
[[Category: Rhodobacter sphaeroides]]
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[[Category: photosynthetic reaction center]]
[[Category: photosynthetic reaction center]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:14:10 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:10:47 2008''

Revision as of 17:10, 20 March 2008

Image:4rcr.jpg


PDB ID 4rcr

Drag the structure with the mouse to rotate
, resolution 2.8Å
Ligands: , , , and
Coordinates: save as pdb, mmCIF, xml



STRUCTURE OF THE REACTION CENTER FROM RHODOBACTER SPHAEROIDES R-26 AND 2.4.1: PROTEIN-COFACTOR (BACTERIOCHLOROPHYLL, BACTERIOPHEOPHYTIN, AND CAROTENOID) INTERACTIONS


Overview

The three-dimensional structures of the cofactors and protein subunits of the reaction center (RC) from the carotenoidless mutant strain of Rhodobacter sphaeroides R-26 and the wild-type strain 2.4.1 have been determined by x-ray diffraction to resolutions of 2.8 A and 3.0 A with R values of 24% and 26%, respectively. The bacteriochlorophyll dimer (D), bacteriochlorophyll monomers (B), and bacteriopheophytin monomers (phi) form two branches, A and B, that are approximately related by a twofold symmetry axis. The cofactors are located in hydrophobic environments formed by the L and M subunits. Differences in the cofactor-protein interactions between the A and B cofactors, as well as between the corresponding cofactors of Rb, sphaeroides and Rhodopseudomonas viridis [Michel, H., Epp, O. & Deisenhofer, J. (1986) EMBO J. 3, 2445-2451], are delineated. The roles of several structural features in the preferential electron transfer along the A branch are discussed. Two bound detergent molecules of beta-octyl glucoside have been located near BA and BB. The environment of the carotenoid, C, that is present in RCs from Rb. sphaeroides 2.4.1 consists largely of aromatic residues of the M subunit. A role of BB in the triplet energy transfer from D to C and the reason for the preferential ease of removal of BB from the RC is proposed.

About this Structure

4RCR is a Protein complex structure of sequences from Rhodobacter sphaeroides. Full crystallographic information is available from OCA.

Reference

Structure of the reaction center from Rhodobacter sphaeroides R-26 and 2.4.1: protein-cofactor (bacteriochlorophyll, bacteriopheophytin, and carotenoid) interactions., Yeates TO, Komiya H, Chirino A, Rees DC, Allen JP, Feher G, Proc Natl Acad Sci U S A. 1988 Nov;85(21):7993-7. PMID:3186702

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