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1apb

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A PRO TO GLY MUTATION IN THE HINGE OF THE ARABINOSE-BINDING PROTEIN ENHANCES BINDING AND ALTERS SPECIFICITY: SUGAR-BINDING AND CRYSTALLOGRAPHIC STUDIES

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

Categories: Escherichia coli | Large Structures | Quiocho FA | Tesmer JJG | Vermersch PS

@@ Line 1: / Line 1: @@
-[[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==
+==A PRO TO GLY MUTATION IN THE HINGE OF THE ARABINOSE-BINDING PROTEIN ENHANCES BINDING AND ALTERS SPECIFICITY: SUGAR-BINDING AND CRYSTALLOGRAPHIC STUDIES==
-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.
+<StructureSection load='1apb' size='340' side='right'caption='[[1apb]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
+== Structural highlights ==
-==About this Structure==
+<table><tr><td colspan='2'>[[1apb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1APB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1APB FirstGlance]. <br>
-APB 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].
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.76&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FCA:ALPHA-D-FUCOSE'>FCA</scene>, <scene name='pdbligand=FCB:BETA-D-FUCOSE'>FCB</scene></td></tr>
-==Reference==
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1apb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1apb OCA], [https://pdbe.org/1apb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1apb RCSB], [https://www.ebi.ac.uk/pdbsum/1apb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1apb ProSAT]</span></td></tr>
-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]
+</table>
+== Function ==
+[https://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]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ap/1apb_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1apb ConSurf].
+<div style="clear:both"></div>
+__TOC__
+</StructureSection>
 [[Category: Escherichia coli]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Quiocho, F.A.]]
+[[Category: Quiocho FA]]
-[[Category: Tesmer, J.J.G.]]
+[[Category: Tesmer JJG]]
-[[Category: Vermersch, P.S.]]
+[[Category: Vermersch PS]]
-[[Category: binding proteins]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:01:17 2007''

1apb

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A PRO TO GLY MUTATION IN THE HINGE OF THE ARABINOSE-BINDING PROTEIN ENHANCES BINDING AND ALTERS SPECIFICITY: SUGAR-BINDING AND CRYSTALLOGRAPHIC STUDIES

Structural highlights

Function

Evolutionary Conservation

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