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1pst

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[[Image:1pst.gif|left|200px]]
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{{Seed}}
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[[Image:1pst.png|left|200px]]
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{{STRUCTURE_1pst| PDB=1pst | SCENE= }}
{{STRUCTURE_1pst| PDB=1pst | SCENE= }}
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'''CRYSTALLOGRAPHIC ANALYSES OF SITE-DIRECTED MUTANTS OF THE PHOTOSYNTHETIC REACTION CENTER FROM RHODOBACTER SPHAEROIDES'''
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===CRYSTALLOGRAPHIC ANALYSES OF SITE-DIRECTED MUTANTS OF THE PHOTOSYNTHETIC REACTION CENTER FROM RHODOBACTER SPHAEROIDES===
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==Overview==
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Seven site-directed mutants of the bacterial photosynthetic reaction center (RC) from the 2.4.1 and WS 231 wild-type strains of Rhodobacter sphaeroides have been crystallized and their X-ray diffraction analyzed to resolutions between 3.0 and 4.0 A. The mutations can be divided into four distinct categories: (1) mutations altering cofactor composition that affect electron transfer and quantum yield, His M202--&gt;Leu (M202HL), His L173--&gt;Leu (L173HL), and Leu M214--&gt;His (M214LH); (2) a mutation in the proposed pathway of electron transfer altering electron-transfer kinetics, Tyr M210--&gt;Phe (M210YF); (3) a mutation around the non-heme iron resulting in an iron-less reaction center, His M219--&gt;Cys (M219HC); and (4) mutations around the secondary electron acceptor, a ubiquinone, affecting proton transfer and quinone turnover, Glu L212--&gt;Gln (L212EQ) and Asp L213--&gt;Asn (L213DN). Residues L173 and M202 are within bonding distance of the respective magnesiums of the two bacteriochlorophylls of the BChl special pair, while M214 is close to the bacteriopheophytin on the active A branch of the RC. The L173HL and M202HL crystal structures show that the respective bacteriochlorophylls are replaced with bacteriopheophytins (i.e., loss of magnesium) without significant structural perturbations to the surrounding main-chain or side-chain atoms. In the M214LH mutant, the bacteriopheophytin has been replaced by a bacteriochlorophyll, and the side chain of His M214 is within ligand distance of the magnesium. The M210YF, L212EQ, and L213DN mutants show no significant tertiary structure changes near the mutation sites. The M219HC diffraction data indicate that the overall tertiary structure of the reaction center is maintained in the absence of the non-heme iron.
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{{ABSTRACT_PUBMED_8161514}}
==About this Structure==
==About this Structure==
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[[Category: Rees, D C.]]
[[Category: Rees, D C.]]
[[Category: Photosynthetic reaction center]]
[[Category: Photosynthetic reaction center]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:26:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:14:31 2008''

Revision as of 11:14, 29 July 2008

Image:1pst.png

Template:STRUCTURE 1pst

CRYSTALLOGRAPHIC ANALYSES OF SITE-DIRECTED MUTANTS OF THE PHOTOSYNTHETIC REACTION CENTER FROM RHODOBACTER SPHAEROIDES

Template:ABSTRACT PUBMED 8161514

About this Structure

1PST is a Protein complex structure of sequences from Rhodobacter sphaeroides. Full crystallographic information is available from OCA.

Reference

Crystallographic analyses of site-directed mutants of the photosynthetic reaction center from Rhodobacter sphaeroides., Chirino AJ, Lous EJ, Huber M, Allen JP, Schenck CC, Paddock ML, Feher G, Rees DC, Biochemistry. 1994 Apr 19;33(15):4584-93. PMID:8161514

Page seeded by OCA on Tue Jul 29 14:14:31 2008

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