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1ap9
From Proteopedia
| 1ap9, resolution 2.35Å () | |||||||||
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| Domains: | Bac_rhodopsin | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
X-RAY STRUCTURE OF BACTERIORHODOPSIN FROM MICROCRYSTALS GROWN IN LIPIDIC CUBIC PHASES
Lipidic cubic phases provide a continuous three-dimensional bilayer matrix that facilitates nucleation and growth of bacteriorhodopsin microcrystals. The crystals diffract x-rays isotropically to 2.0 angstroms. The structure of this light-driven proton pump was solved at a resolution of 2.5 angstroms by molecular replacement, using previous results from electron crystallographic studies as a model. The earlier structure was generally confirmed, but several differences were found, including loop conformations and side chain residues. Eight water molecules are now identified experimentally in the proton pathway. These findings reveal the constituents of the proton translocation pathway in the ground state.
X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases., Pebay-Peyroula E, Rummel G, Rosenbusch JP, Landau EM, Science. 1997 Sep 12;277(5332):1676-81. PMID:9287223
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1AP9 is a 1 chain structure of sequence from Halobacterium salinarum. Full crystallographic information is available from OCA.
Reference
- Pebay-Peyroula E, Rummel G, Rosenbusch JP, Landau EM. X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases. Science. 1997 Sep 12;277(5332):1676-81. PMID:9287223
Page seeded by OCA on Mon Feb 16 12:18:30 2009
