1q5i
From Proteopedia
| Line 7: | Line 7: | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= BOP OR VNG1467G ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2242 Halobacterium salinarum]) | |GENE= BOP OR VNG1467G ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2242 Halobacterium salinarum]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1q5j|1Q5J]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1q5i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q5i OCA], [http://www.ebi.ac.uk/pdbsum/1q5i PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1q5i RCSB]</span> | ||
}} | }} | ||
| Line 27: | Line 30: | ||
[[Category: Yang, D.]] | [[Category: Yang, D.]] | ||
[[Category: Yohannan, S.]] | [[Category: Yohannan, S.]] | ||
| - | [[Category: RET]] | ||
[[Category: alpha helix]] | [[Category: alpha helix]] | ||
[[Category: membrane protein]] | [[Category: membrane protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:09:12 2008'' |
Revision as of 20:09, 30 March 2008
| |||||||
| , resolution 2.3Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | BOP OR VNG1467G (Halobacterium salinarum) | ||||||
| Related: | 1Q5J
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of bacteriorhodopsin mutant P186A crystallized from bicelles
Overview
One of the hallmarks of membrane protein structure is the high frequency of transmembrane helix kinks, which commonly occur at proline residues. Because the proline side chain usually precludes normal helix geometry, it is reasonable to expect that proline residues generate these kinks. We observe, however, that the three prolines in bacteriorhodopsin transmembrane helices can be changed to alanine with little structural consequences. This finding leads to a conundrum: if proline is not required for helix bending, why are prolines commonly present at bends in transmembrane helices? We propose an evolutionary hypothesis in which a mutation to proline initially induces the kink. The resulting packing defects are later repaired by further mutation, thereby locking the kink in the structure. Thus, most prolines in extant proteins can be removed without major structural consequences. We further propose that nonproline kinks are places where vestigial prolines were later removed during evolution. Consistent with this hypothesis, at 14 of 17 nonproline kinks in membrane proteins of known structure, we find prolines in homologous sequences. Our analysis allows us to predict kink positions with >90% reliability. Kink prediction indicates that different G protein-coupled receptor proteins have different kink patterns and therefore different structures.
About this Structure
1Q5I is a Single protein structure of sequence from Halobacterium salinarum. Full crystallographic information is available from OCA.
Reference
The evolution of transmembrane helix kinks and the structural diversity of G protein-coupled receptors., Yohannan S, Faham S, Yang D, Whitelegge JP, Bowie JU, Proc Natl Acad Sci U S A. 2004 Jan 27;101(4):959-63. Epub 2004 Jan 19. PMID:14732697
Page seeded by OCA on Sun Mar 30 23:09:12 2008
