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2jiy

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{{STRUCTURE_2jiy| PDB=2jiy | SCENE= }}
{{STRUCTURE_2jiy| PDB=2jiy | SCENE= }}
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'''PHOTOSYNTHETIC REACTION CENTER MUTANT WITH ALA M149 REPLACED WITH TRP (CHAIN M, AM149W)'''
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===PHOTOSYNTHETIC REACTION CENTER MUTANT WITH ALA M149 REPLACED WITH TRP (CHAIN M, AM149W)===
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==Overview==
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X-ray crystallography has been used to investigate the extent of structural changes in mutants of the purple bacterial reaction center that assemble without a particular ubiquinone or bacteriopheophytin cofactor. In the case of the bacteriopheophytin-exclusion mutant, in which Ala M149 was replaced by Trp (AM149W), the quality of protein crystals was improved over that seen in previous work by minimizing illumination, time, and temperature during the purification protocol and carrying out crystal growth at 4 degrees C after overnight incubation at 18 degrees C. The X-ray crystal structure of the AM149W mutant, determined to a resolution of 2.2 A, showed very little change in protein structure despite the absence of the bacteriopheophytin cofactor. Changes in the electron density map in the region of the cofactor binding site could be accounted for by changes in the conformation of the phytol side chains of adjacent cofactors and the presence of a buried water molecule. Residues lining the vacated binding pocket did not show any significant changes in conformation or increases in disorder as assessed through crystallographic atomic displacement parameters (B-factors). The X-ray crystal structure of a reaction center lacking the primary acceptor ubiquinone through mutation of Ala M248 to Trp (AM248W) was also determined, to a resolution of 2.8 A. Again, despite the absence of an internal cofactor only very minor changes in protein structure were observed. This is in contrast to a previous report on a reaction center lacking this ubiquinone through mutation of Ala M260 to Trp (AM260W) where more extensive changes in structure were apparent. All three mutant reaction centers showed a decrease in thermal stability when housed in the native membrane, but this decrease was smaller for the AM260W mutant than the AM248W complex, possibly due to beneficial effects of the observed changes in protein structure. The lack of major changes in protein structure despite the absence of large internal cofactors is discussed in terms of protein rigidity, the protective influence of the adaptable membrane environment, and the role of small molecules and ions as packing material in the internal cavities created by this type of mutation.
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{{ABSTRACT_PUBMED_17711306}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Structural responses to cavity-creating mutations in an integral membrane protein., Fyfe PK, Potter JA, Cheng J, Williams CM, Watson AJ, Jones MR, Biochemistry. 2007 Sep 18;46(37):10461-72. Epub 2007 Aug 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17711306 17711306]
Structural responses to cavity-creating mutations in an integral membrane protein., Fyfe PK, Potter JA, Cheng J, Williams CM, Watson AJ, Jones MR, Biochemistry. 2007 Sep 18;46(37):10461-72. Epub 2007 Aug 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17711306 17711306]
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On the role of basic residues in adapting the reaction centre-LH1 complex for growth at elevated temperatures in purple bacteria., Watson AJ, Hughes AV, Fyfe PK, Wakeham MC, Holden-Dye K, Heathcote P, Jones MR, Photosynth Res. 2005 Nov;86(1-2):81-100. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16172928 16172928]
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Structural details of an interaction between cardiolipin and an integral membrane protein., McAuley KE, Fyfe PK, Ridge JP, Isaacs NW, Cogdell RJ, Jones MR, Proc Natl Acad Sci U S A. 1999 Dec 21;96(26):14706-11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10611277 10611277]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Rhodobacter sphaeroides]]
[[Category: Rhodobacter sphaeroides]]
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[[Category: Transmembrane]]
[[Category: Transmembrane]]
[[Category: Transport]]
[[Category: Transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 14:45:22 2008''

Revision as of 11:45, 28 July 2008

Image:2jiy.png

Template:STRUCTURE 2jiy

PHOTOSYNTHETIC REACTION CENTER MUTANT WITH ALA M149 REPLACED WITH TRP (CHAIN M, AM149W)

Template:ABSTRACT PUBMED 17711306

About this Structure

2JIY is a Protein complex structure of sequences from Rhodobacter sphaeroides. Full crystallographic information is available from OCA.

Reference

Structural responses to cavity-creating mutations in an integral membrane protein., Fyfe PK, Potter JA, Cheng J, Williams CM, Watson AJ, Jones MR, Biochemistry. 2007 Sep 18;46(37):10461-72. Epub 2007 Aug 21. PMID:17711306

On the role of basic residues in adapting the reaction centre-LH1 complex for growth at elevated temperatures in purple bacteria., Watson AJ, Hughes AV, Fyfe PK, Wakeham MC, Holden-Dye K, Heathcote P, Jones MR, Photosynth Res. 2005 Nov;86(1-2):81-100. PMID:16172928

Structural details of an interaction between cardiolipin and an integral membrane protein., McAuley KE, Fyfe PK, Ridge JP, Isaacs NW, Cogdell RJ, Jones MR, Proc Natl Acad Sci U S A. 1999 Dec 21;96(26):14706-11. PMID:10611277

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