1c3w: Difference between revisions
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|PDB= 1c3w |SIZE=350|CAPTION= <scene name='initialview01'>1c3w</scene>, resolution 1.55Å | |PDB= 1c3w |SIZE=350|CAPTION= <scene name='initialview01'>1c3w</scene>, resolution 1.55Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=LI1:1-[2,6,10.14-TETRAMETHYL-HEXADECAN-16-YL]-2-[2,10,14-TRIMETHYLHEXADECAN-16-YL]GLYCEROL'>LI1</scene>, <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=LI1:1-[2,6,10.14-TETRAMETHYL-HEXADECAN-16-YL]-2-[2,10,14-TRIMETHYLHEXADECAN-16-YL]GLYCEROL'>LI1</scene>, <scene name='pdbligand=RET:RETINAL'>RET</scene>, <scene name='pdbligand=SQU:2,10,23-TRIMETHYL-TETRACOSANE'>SQU</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1brx|1BRX]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1c3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c3w OCA], [http://www.ebi.ac.uk/pdbsum/1c3w PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1c3w RCSB]</span> | |||
}} | }} | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Luecke, H.]] | [[Category: Luecke, H.]] | ||
[[Category: 7-transmembrane]] | [[Category: 7-transmembrane]] | ||
[[Category: haloarchaea]] | [[Category: haloarchaea]] | ||
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[[Category: serpentine]] | [[Category: serpentine]] | ||
''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 19:14:00 2008'' | ||
Revision as of 19:14, 30 March 2008
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| , resolution 1.55Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Related: | 1BRX
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
BACTERIORHODOPSIN/LIPID COMPLEX AT 1.55 A RESOLUTION
OverviewOverview
Th?e atomic structure of the light-driven ion pump bacteriorhodopsin and the surrounding lipid matrix was determined by X-ray diffraction of crystals grown in cubic lipid phase. In the extracellular region, an extensive three-dimensional hydrogen-bonded network of protein residues and seven water molecules leads from the buried retinal Schiff base and the proton acceptor Asp85 to the membrane surface. Near Lys216 where the retinal binds, transmembrane helix G contains a pi-bulge that causes a non-proline? kink. The bulge is stabilized by hydrogen-bonding of the main-chain carbonyl groups of Ala215 and Lys216 with two buried water molecules located between the Schiff base and the proton donor Asp96 in the cytoplasmic region. The results indicate extensive involvement of bound water molecules in both the structure and the function of this seven-helical membrane protein. A bilayer of 18 tightly bound lipid chains forms an annulus around the protein in the crystal. Contacts between the trimers in the membrane plane are mediated almost exclusively by lipids.
About this StructureAbout this Structure
1C3W is a Single protein structure of sequence from Halobacterium salinarum. The following page contains interesting information on the relation of 1C3W with [Bacteriorhodopsin]. Full crystallographic information is available from OCA.
ReferenceReference
Structure of bacteriorhodopsin at 1.55 A resolution., Luecke H, Schobert B, Richter HT, Cartailler JP, Lanyi JK, J Mol Biol. 1999 Aug 27;291(4):899-911. PMID:10452895
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