1p8h
From Proteopedia
Line 4: | Line 4: | ||
|PDB= 1p8h |SIZE=350|CAPTION= <scene name='initialview01'>1p8h</scene>, resolution 1.52Å | |PDB= 1p8h |SIZE=350|CAPTION= <scene name='initialview01'>1p8h</scene>, resolution 1.52Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= | + | |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= BOP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2242 Halobacterium salinarum]) | |GENE= BOP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2242 Halobacterium salinarum]) | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY=[[1c3w|1C3W]], [[1m0l|1M0L]], [[1m0k|1M0K]], [[1m0m|1M0M]], [[1o0a|1O0A]], [[1p8i|1P8I]], [[1p8u|1P8U]] | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1p8h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p8h OCA], [http://www.ebi.ac.uk/pdbsum/1p8h PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1p8h RCSB]</span> | ||
}} | }} | ||
Line 23: | Line 26: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Lanyi, J K.]] | [[Category: Lanyi, J K.]] | ||
- | [[Category: LI1]] | ||
- | [[Category: RET]] | ||
- | [[Category: SQU]] | ||
[[Category: 7-transmembrane]] | [[Category: 7-transmembrane]] | ||
[[Category: haloarchaea]] | [[Category: haloarchaea]] | ||
Line 36: | Line 36: | ||
[[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 22:56:20 2008'' |
Revision as of 19:56, 30 March 2008
| |||||||
, resolution 1.52Å | |||||||
---|---|---|---|---|---|---|---|
Ligands: | , , | ||||||
Gene: | BOP (Halobacterium salinarum) | ||||||
Related: | 1C3W, 1M0L, 1M0K, 1M0M, 1O0A, 1P8I, 1P8U
| ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
BACTERIORHODOPSIN M1 INTERMEDIATE PRODUCED AT ROOM TEMPERATURE
Overview
An M intermediate of wild-type bacteriorhodopsin and an N intermediate of the V49A mutant were accumulated in photostationary states at pH 5.6 and 295 K, and their crystal structures determined to 1.52A and 1.62A resolution, respectively. They appear to be M(1) and N' in the sequence, M(1)<-->M(2)<-->M'(2)<-->N<-->N'-->O-->BR, where M(1), M(2), and M'(2) contain an unprotonated retinal Schiff base before and after a reorientation switch and after proton release to the extracellular surface, while N and N' contain a reprotonated Schiff base, before and after reprotonation of Asp96 from the cytoplasmic surface. In M(1), we detect a cluster of three hydrogen-bonded water molecules at Asp96, not present in the BR state. In M(2), whose structure we reported earlier, one of these water molecules intercalates between Asp96 and Thr46. In N', the cluster is transformed into a single-file hydrogen-bonded chain of four water molecules that connects Asp96 to the Schiff base. We find a network of three water molecules near residue 219 in the crystal structure of the non-illuminated F219L mutant, where the residue replacement creates a cavity. This suggests that the hydration of the cytoplasmic region we observe in N' might have occurred spontaneously, beginning at an existing water molecule as nucleus, in the cavities from residue rearrangements in the photocycle.
About this Structure
1P8H is a Single protein structure of sequence from Halobacterium salinarum. Full crystallographic information is available from OCA.
Reference
Crystallographic structures of the M and N intermediates of bacteriorhodopsin: assembly of a hydrogen-bonded chain of water molecules between Asp-96 and the retinal Schiff base., Schobert B, Brown LS, Lanyi JK, J Mol Biol. 2003 Jul 11;330(3):553-70. PMID:12842471
Page seeded by OCA on Sun Mar 30 22:56:20 2008