View source for 1apb

[[Image:1apb.gif|left|200px]]<br /><applet load="1apb" size="450" color="white" frame="true" align="right" spinBox="true" 
caption="1apb, resolution 1.76&Aring;" />
'''A PRO TO GLY MUTATION IN THE HINGE OF THE ARABINOSE-BINDING PROTEIN ENHANCES BINDING AND ALTERS SPECIFICITY: SUGAR-BINDING AND CRYSTALLOGRAPHIC STUDIES'''<br />

==Overview==
The L-arabinose-binding protein (ABP) of Escherichia coli consists, structurally of two distinct globular domains connected by a hinge of, three separate peptide segments. Arabinose is bound and completely, sequestered within the deep cleft between the two domains. With reduced, affinity, ABP also binds D-galactose (approximately 2-fold reduction) and, D-fucose (approximately 40-fold reduction). Experiments have been, conducted to explore the role in sugar binding of the hinge connecting the, two domains of ABP. To increase the flexibility of the hinge region, a, glycine was substituted for a proline at position 254 by site-directed, mutagenesis. Unexpectedly, this mutation resulted in the dramatic, enhancement of galactose binding over that of arabinose. The affinity of, the mutant ABP for galactose increased by over 20-fold, while that for, arabinose and fucose remained relatively unchanged. We have measured, association and dissociation rates of the Gly-254 ABP with L-arabinose, D-galactose, and D-fucose and have determined the crystallographic, structure of the protein complexed with each of the three sugars. Both the, ligand-binding kinetic measurements and structure analysis indicate that, the altered specificity is due to an effective increase in the rigidity of, the hinge in the closed conformation which is induced upon galactose, binding. Stabilizing contacts are formed between the strands of the hinge, in the Gly-254 ABP when galactose is bound which are not found in, complexes with the other sugars or the liganded wild-type protein.

==About this Structure==
1APB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1APB OCA]. 

==Reference==
A Pro to Gly mutation in the hinge of the arabinose-binding protein enhances binding and alters specificity. Sugar-binding and crystallographic studies., Vermersch PS, Tesmer JJ, Lemon DD, Quiocho FA, J Biol Chem. 1990 Sep 25;265(27):16592-603. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2204627 2204627]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Quiocho, F.A.]]
[[Category: Tesmer, J.J.G.]]
[[Category: Vermersch, P.S.]]
[[Category: binding proteins]]

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