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| - | [[Image:1umx.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1umx.png|left|200px]] |
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| | {{STRUCTURE_1umx| PDB=1umx | SCENE= }} | | {{STRUCTURE_1umx| PDB=1umx | SCENE= }} |
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| - | '''PHOTOSYNTHETIC REACTION CENTER MUTANT WITH ARG M267 REPLACED WITH LEU (CHAIN M, R267L)'''
| + | ===PHOTOSYNTHETIC REACTION CENTER MUTANT WITH ARG M267 REPLACED WITH LEU (CHAIN M, R267L)=== |
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| - | ==Overview==
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| - | Relatively little is known about the functions of specific molecular interactions between membrane proteins and membrane lipids. The structural and functional consequences of disrupting a previously identified interaction between a molecule of the diacidic lipid cardiolipin and the purple bacterial reaction centre were examined. Mutagenesis of a highly conserved arginine (M267) that is responsible for binding the head-group of the cardiolipin (to leucine) did not affect the rate of photosynthetic growth, the functional properties of the reaction centre, or the X-ray crystal structure of the complex (determined to a resolution of 2.8 A). However, the thermal stability of the protein was compromised by this mutation, part of the reaction centre population showing an approximately 5 degrees C decrease in melting temperature in response to the arginine to leucine mutation. The crystallised mutant reaction centre also no longer bound detectable amounts of cardiolipin at this site. Taken together, these observations suggest that this particular protein-lipid interaction contributes to the thermal stability of the complex, at least when in detergent micelles. These findings are discussed in the light of proposals concerning the unfolding processes that occur when membrane proteins are heated, and we propose that one function of the cardiolipin is to stabilise the interaction between adjacent membrane-spanning alpha-helices in a region where there are no direct protein-protein interactions.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_14741581}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 14741581 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_14741581}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Photosynthetic reaction center]] | | [[Category: Photosynthetic reaction center]] |
| | [[Category: Transmembrane]] | | [[Category: Transmembrane]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:26:46 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:08:57 2008'' |
Revision as of 01:08, 28 July 2008
Template:STRUCTURE 1umx
PHOTOSYNTHETIC REACTION CENTER MUTANT WITH ARG M267 REPLACED WITH LEU (CHAIN M, R267L)
Template:ABSTRACT PUBMED 14741581
About this Structure
1UMX is a Protein complex structure of sequences from Rhodobacter sphaeroides. Full crystallographic information is available from OCA.
Reference
Disruption of a specific molecular interaction with a bound lipid affects the thermal stability of the purple bacterial reaction centre., Fyfe PK, Isaacs NW, Cogdell RJ, Jones MR, Biochim Biophys Acta. 2004 Jan 30;1608(1):11-22. PMID:14741581
Page seeded by OCA on Mon Jul 28 04:08:57 2008
