2ntu: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:2ntu.jpg|left|200px]] | [[Image:2ntu.jpg|left|200px]] | ||
'''Bacteriorhodopsin, wild type, before illumination''' | {{Structure | ||
|PDB= 2ntu |SIZE=350|CAPTION= <scene name='initialview01'>2ntu</scene>, resolution 1.53Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=RET:RETINAL'>RET</scene> | |||
|ACTIVITY= | |||
|GENE= bop ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2242 Halobacterium salinarum]) | |||
}} | |||
'''Bacteriorhodopsin, wild type, before illumination''' | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
2NTU is a [ | 2NTU 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=2NTU OCA]. | ||
==Reference== | ==Reference== | ||
Structural changes in the L photointermediate of bacteriorhodopsin., Lanyi JK, Schobert B, J Mol Biol. 2007 Feb 2;365(5):1379-92. Epub 2006 Nov 10. PMID:[http:// | Structural changes in the L photointermediate of bacteriorhodopsin., Lanyi JK, Schobert B, J Mol Biol. 2007 Feb 2;365(5):1379-92. Epub 2006 Nov 10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17141271 17141271] | ||
[[Category: Halobacterium salinarum]] | [[Category: Halobacterium salinarum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 20: | Line 29: | ||
[[Category: ion pump]] | [[Category: ion pump]] | ||
[[Category: ion transport]] | [[Category: ion transport]] | ||
[[Category: | [[Category: lipid]] | ||
[[Category: membrane protein]] | [[Category: membrane protein]] | ||
[[Category: photoreceptor]] | [[Category: photoreceptor]] | ||
| Line 26: | Line 35: | ||
[[Category: serpentine]] | [[Category: serpentine]] | ||
''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 17:51:04 2008'' | ||
Revision as of 18:51, 20 March 2008
| |||||||
| , resolution 1.53Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | bop (Halobacterium salinarum) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Bacteriorhodopsin, wild type, before illumination
OverviewOverview
The L to M reaction of the bacteriorhodopsin photocycle includes the crucial proton transfer from the retinal Schiff base to Asp85. In spite of the importance of the L state in deciding central issues of the transport mechanism in this pump, the serious disagreements among the three published crystallographic structures of L have remained unresolved. Here, we report on the X-ray diffraction structure of the L state, to 1.53-1.73 A resolutions, from replicate data sets collected from six independent crystals. Unlike earlier studies, the partial occupancy refinement uses diffraction intensities from the same crystals before and after the illumination to produce the trapped L state. The high reproducibility of inter-atomic distances, and bond angles and torsions of the retinal, lends credibility to the structural model. The photoisomerized 13-cis retinal in L is twisted at the C(13)=C(14) and C(15)=NZ double-bonds, and the Schiff base does not lose its connection to Wat402 and, therefore, to the proton acceptor Asp85. The protonation of Asp85 by the Schiff base in the L-->M reaction is likely to occur, therefore, via Wat402. It is evident from the structure of the L state that various conformational changes involving hydrogen-bonding residues and bound water molecules begin to propagate from the retinal to the protein at this stage already, and in both extracellular and cytoplasmic directions. Their rationales in the transport can be deduced from the way their amplitudes increase in the intermediates that follow L in the reaction cycle, and from the proton transfer reactions with which they are associated.
About this StructureAbout this Structure
2NTU is a Single protein structure of sequence from Halobacterium salinarum. Full crystallographic information is available from OCA.
ReferenceReference
Structural changes in the L photointermediate of bacteriorhodopsin., Lanyi JK, Schobert B, J Mol Biol. 2007 Feb 2;365(5):1379-92. Epub 2006 Nov 10. PMID:17141271
Page seeded by OCA on Thu Mar 20 17:51:04 2008