1abf: Difference between revisions

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[[Image:1abf.jpg|left|200px]]
[[Image:1abf.jpg|left|200px]]


{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1abf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1abf OCA], [http://www.ebi.ac.uk/pdbsum/1abf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1abf RCSB]</span>
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'''SUBSTRATE SPECIFICITY AND AFFINITY OF A PROTEIN MODULATED BY BOUND WATER MOLECULES'''
'''SUBSTRATE SPECIFICITY AND AFFINITY OF A PROTEIN MODULATED BY BOUND WATER MOLECULES'''
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[[Category: Quiocho, F A.]]
[[Category: Quiocho, F A.]]
[[Category: Wilson, D K.]]
[[Category: Wilson, D K.]]
[[Category: binding protein]]
[[Category: Binding protein]]
 
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:37:02 2008''

Revision as of 10:04, 2 May 2008

File:1abf.jpg

Template:STRUCTURE 1abf

SUBSTRATE SPECIFICITY AND AFFINITY OF A PROTEIN MODULATED BY BOUND WATER MOLECULES


OverviewOverview

Water molecules influence molecular interactions in all biological systems, yet it is extremely difficult to understand their effects in precise atomic detail. Here we present evidence, based on highly refined atomic structures of the complexes of the L-arabinose-binding protein with L-arabinose, D-fucose and D-galactose, that bound water molecules, coupled with localized conformational changes, can govern substrate specificity and affinity. The atoms common to the three sugars are identically positioned in the binding site and the same nine strong hydrogen bonds are formed in all three complexes. Two hydrogen-bonded water molecules in the site contribute further to tight binding of L-arabinose but create an unfavourable interaction with the methyl group of D-fucose. Equally tight binding of D-galactose is attained by the replacement of one of the hydrogen-bonded water molecules by its--CH2OH group, coordinated with localized structural changes which include a shift and redirection of the hydrogen-bonding interactions of the other water molecule. These observations illustrate how ordered water molecules can contribute directly to the properties of proteins by influencing their interaction with ligands.

About this StructureAbout this Structure

1ABF is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Substrate specificity and affinity of a protein modulated by bound water molecules., Quiocho FA, Wilson DK, Vyas NK, Nature. 1989 Aug 3;340(6232):404-7. PMID:2818726 Page seeded by OCA on Fri May 2 10:04:31 2008

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