1tn0
From Proteopedia
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| - | [[Image:1tn0.gif|left|200px]] | + | [[Image:1tn0.gif|left|200px]] |
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| - | '''Structure of bacterorhodopsin mutant A51P''' | + | {{Structure |
| + | |PDB= 1tn0 |SIZE=350|CAPTION= <scene name='initialview01'>1tn0</scene>, resolution 2.50Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=RET:RETINAL'>RET</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= BOP, VNG1467G ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2242 Halobacterium salinarum]) | ||
| + | }} | ||
| + | |||
| + | '''Structure of bacterorhodopsin mutant A51P''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1TN0 is a [ | + | 1TN0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Halobacterium_salinarum Halobacterium salinarum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TN0 OCA]. |
==Reference== | ==Reference== | ||
| - | Proline substitutions are not easily accommodated in a membrane protein., Yohannan S, Yang D, Faham S, Boulting G, Whitelegge J, Bowie JU, J Mol Biol. 2004 Jul 30;341(1):1-6. PMID:[http:// | + | Proline substitutions are not easily accommodated in a membrane protein., Yohannan S, Yang D, Faham S, Boulting G, Whitelegge J, Bowie JU, J Mol Biol. 2004 Jul 30;341(1):1-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15312757 15312757] |
[[Category: Halobacterium salinarum]] | [[Category: Halobacterium salinarum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: membrane protein]] | [[Category: membrane protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:20:34 2008'' |
Revision as of 12:20, 20 March 2008
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| , resolution 2.50Å | |||||||
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| Ligands: | |||||||
| Gene: | BOP, VNG1467G (Halobacterium salinarum) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of bacterorhodopsin mutant A51P
Overview
Proline residues are relatively common in transmembrane helices. This suggests that proline substitutions may be readily tolerated in membrane proteins, even though they invariably produce deviations from canonical helical structure. We have experimentally tested this possibility by making proline substitutions at 15 positions throughout the N-terminal half of bacteriorhodopsin helix B. We find that six of the substitutions yielded no active protein and all the others were destabilizing. Three mutations were only slightly destabilizing, however, reducing stability by about 0.5 kcal/mol, and these all occurred close to the N terminus. This result is consistent with the observation that proline is more common near the ends of TM helices. To learn how proline side-chains could be structurally accommodated at different locations in the helix, we solved the structures of a moderately destabilized mutant positioned near the N terminus of the helix, K41P, and a severely destabilized mutant positioned near the middle of the helix, A51P. The K41P mutation produced only local structural alterations, while the A51P mutation resulted in small, but widely distributed structural changes in helix B. Our results indicate that proline is not easily accommodated in transmembrane helices and that the tolerance to proline substitution is dependent, in a complex way, on the position in the structure.
About this Structure
1TN0 is a Single protein structure of sequence from Halobacterium salinarum. Full crystallographic information is available from OCA.
Reference
Proline substitutions are not easily accommodated in a membrane protein., Yohannan S, Yang D, Faham S, Boulting G, Whitelegge J, Bowie JU, J Mol Biol. 2004 Jul 30;341(1):1-6. PMID:15312757
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