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| | {{STRUCTURE_1gzm| PDB=1gzm | SCENE= }} | | {{STRUCTURE_1gzm| PDB=1gzm | SCENE= }} |
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| - | '''STRUCTURE OF BOVINE RHODOPSIN IN A TRIGONAL CRYSTAL FORM'''
| + | ===STRUCTURE OF BOVINE RHODOPSIN IN A TRIGONAL CRYSTAL FORM=== |
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| - | ==Overview==
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| - | We have determined the structure of bovine rhodopsin at 2.65 A resolution using untwinned native crystals in the space group P3(1), by molecular replacement from the 2.8 A model (1F88) solved in space group P4(1). The new structure reveals mechanistically important details unresolved previously, which are considered in the membrane context by docking the structure into a cryo-electron microscopy map of 2D crystals. Kinks in the transmembrane helices facilitate inter-helical polar interactions. Ordered water molecules extend the hydrogen bonding networks, linking Trp265 in the retinal binding pocket to the NPxxY motif near the cytoplasmic boundary, and the Glu113 counterion for the protonated Schiff base to the extracellular surface. Glu113 forms a complex with a water molecule hydrogen bonded between its main chain and side-chain oxygen atoms. This can be expected to stabilise the salt-bridge with the protonated Schiff base linking the 11-cis-retinal to Lys296. The cytoplasmic ends of helices H5 and H6 have been extended by one turn. The G-protein interaction sites mapped to the cytoplasmic ends of H5 and H6 and a spiral extension of H5 are elevated above the bilayer. There is a surface cavity next to the conserved Glu134-Arg135 ion pair. The cytoplasmic loops have the highest temperature factors in the structure, indicative of their flexibility when not interacting with G protein or regulatory proteins. An ordered detergent molecule is seen wrapped around the kink in H6, stabilising the structure around the potential hinge in H6. These findings provide further explanation for the stability of the dark state structure. They support a mechanism for the activation, initiated by photo-isomerisation of the chromophore to its all-trans form, that involves pivoting movements of kinked helices, which, while maintaining hydrophobic contacts in the membrane interior, can be coupled to amplified translation of the helix ends near the membrane surfaces.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15491621}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15491621 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15491621}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Retinal protein]] | | [[Category: Retinal protein]] |
| | [[Category: Visual pigment]] | | [[Category: Visual pigment]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:13:26 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 06:22:37 2008'' |
Revision as of 03:22, 1 July 2008
Template:STRUCTURE 1gzm
STRUCTURE OF BOVINE RHODOPSIN IN A TRIGONAL CRYSTAL FORM
Template:ABSTRACT PUBMED 15491621
About this Structure
1GZM is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Structure of bovine rhodopsin in a trigonal crystal form., Li J, Edwards PC, Burghammer M, Villa C, Schertler GF, J Mol Biol. 2004 Nov 5;343(5):1409-38. PMID:15491621
Page seeded by OCA on Tue Jul 1 06:22:37 2008
