1abf

From Proteopedia

(Difference between revisions)

Revision as of 06:17, 25 December 2014

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

Structural highlights

1abf is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[ARAF_ECOLI] Involved in the high-affinity L-arabinose membrane transport system. Binds with high affinity to arabinose, but can also bind D-galactose (approximately 2-fold reduction) and D-fucose (approximately 40-fold reduction).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Quiocho FA, Wilson DK, Vyas NK. Substrate specificity and affinity of a protein modulated by bound water molecules. Nature. 1989 Aug 3;340(6232):404-7. PMID:2818726 doi:http://dx.doi.org/10.1038/340404a0

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1abf"

Categories: Escherichia coli | Quiocho, F A | Wilson, D K | Binding protein

@@ Line 6: / Line 6: @@
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1abf RCSB], [http://www.ebi.ac.uk/pdbsum/1abf PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/ARAF_ECOLI ARAF_ECOLI]] Involved in the high-affinity L-arabinose membrane transport system. Binds with high affinity to arabinose, but can also bind D-galactose (approximately 2-fold reduction) and D-fucose (approximately 40-fold reduction).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1abf

From Proteopedia

Revision as of 06:17, 25 December 2014

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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