1glg: Difference between revisions
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<StructureSection load='1glg' size='340' side='right' caption='[[1glg]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1glg' size='340' side='right' caption='[[1glg]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1glg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1glg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GLG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GLG FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene></td></tr> | ||
<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=1glg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1glg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1glg RCSB], [http://www.ebi.ac.uk/pdbsum/1glg PDBsum]</span></td></tr> | <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=1glg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1glg OCA], [http://pdbe.org/1glg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1glg RCSB], [http://www.ebi.ac.uk/pdbsum/1glg PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1glg" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bacillus coli migula 1895]] | ||
[[Category: Quiocho, F A]] | [[Category: Quiocho, F A]] | ||
[[Category: Vyas, M N]] | [[Category: Vyas, M N]] | ||
[[Category: Vyas, N K]] | [[Category: Vyas, N K]] | ||
[[Category: Galactose-binding protein]] | [[Category: Galactose-binding protein]] | ||
Revision as of 21:50, 10 September 2015
CRYSTALLOGRAPHIC ANALYSIS OF THE EPIMERIC AND ANOMERIC SPECIFICITY OF THE PERIPLASMIC TRANSPORT(SLASH)CHEMOTACTIC PROTEIN RECEPTOR FOR D-GLUCOSE AND D-GALACTOSECRYSTALLOGRAPHIC ANALYSIS OF THE EPIMERIC AND ANOMERIC SPECIFICITY OF THE PERIPLASMIC TRANSPORT(SLASH)CHEMOTACTIC PROTEIN RECEPTOR FOR D-GLUCOSE AND D-GALACTOSE
Structural highlights
Function[DGAL_ECOLI] This protein is involved in the active transport of galactose and glucose. It plays a role in the chemotaxis towards the two sugars by interacting with the trg chemoreceptor. 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 PubMedThe D-glucose/D-galactose-binding protein (M(r) = 33,000) found in the periplasm of bacterial cells serves as the primary high-affinity receptor of active transport for and chemotaxis toward both sugar epimers. This protein from Escherichia coli binds D-glucose with a Kd of 2 x 10(-7) M, which is about 2 times tighter than D-galactose. The 2.0-A resolution crystal structure of the binding protein complexed with D-galactose has been refined to a crystallographic R-factor of 0.167. This structure, combined with that previously refined for the complex with D-glucose [Vyas, N.K., Vyas., M. N., & Quiocho, F. A. (1988) Science 242, 1290-1295], provides understanding, in atomic detail, of recognition of sugar epimers and anomers. In the two complex structures, the sugar ring is positioned identically in the binding site, and each hydroxyl group common to both is involved in very similar cooperative hydrogen-bonding interactions with protein residues and ordered water molecules. Only the beta-anomer of both monosaccharides is bound, with Asp154 OD1 primarily responsible for accepting a hydrogen bond from the anomeric hydroxyl. Recognition of both sugar epimers is accomplished principally by hydrogen bonding of Asp14 OD1 with the equatorial OH4 of D-glucose and OD2 with the axial OH4 of D-galactose. These results are reconciled with equilibrium and fast kinetics data, which indicate binding of both anomers of the two sugars, and further compared with sugar recognition by other periplasmic sugar-binding proteins with specificities for arabinose/galactose/fucose, maltooligosaccharides, and ribose. Crystallographic analysis of the epimeric and anomeric specificity of the periplasmic transport/chemosensory protein receptor for D-glucose and D-galactose.,Vyas MN, Vyas NK, Quiocho FA Biochemistry. 1994 Apr 26;33(16):4762-8. PMID:8161535[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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