1s8l: Difference between revisions
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'''Anion-free form of the D85S mutant of bacteriorhodopsin from crystals grown in the presence of halide''' | '''Anion-free form of the D85S mutant of bacteriorhodopsin from crystals grown in the presence of halide''' | ||
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[[Category: Lunde, C S.]] | [[Category: Lunde, C S.]] | ||
[[Category: Rouhani, S.]] | [[Category: Rouhani, S.]] | ||
[[Category: | [[Category: Anion]] | ||
[[Category: | [[Category: Bacteriorhodopsin]] | ||
[[Category: | [[Category: Pump]] | ||
[[Category: | [[Category: X-ray crystallography]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:25:59 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 08:25, 3 May 2008
Anion-free form of the D85S mutant of bacteriorhodopsin from crystals grown in the presence of halide
OverviewOverview
The structure of the D85S mutant of bacteriorhodopsin with a nitrate anion bound in the Schiff base binding site and the structure of the anion-free protein have been obtained in the same crystal form. Together with the previously solved structures of this anion pump, in both the anion-free state and bromide-bound state, these new structures provide insight into how this mutant of bacteriorhodopsin is able to bind a variety of different anions in the same binding pocket. The structural analysis reveals that the main structural change that accommodates different anions is the repositioning of the polar side chain of S85. On the basis of these X-ray crystal structures, the prediction is then made that the D85S/D212N double mutant might bind similar anions and do so over a broader pH range than does the single mutant. Experimental comparison of the dissociation constants, K(d), for a variety of anions confirms this prediction and demonstrates, in addition, that the binding affinity is dramatically improved by the D212N substitution.
About this StructureAbout this Structure
1S8L is a Single protein structure of sequence from Halobacterium sp.. Full crystallographic information is available from OCA.
ReferenceReference
Specificity of anion binding in the substrate pocket of bacteriorhodopsin., Facciotti MT, Cheung VS, Lunde CS, Rouhani S, Baliga NS, Glaeser RM, Biochemistry. 2004 May 4;43(17):4934-43. PMID:15109251 Page seeded by OCA on Sat May 3 08:25:59 2008