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| | <StructureSection load='3ga5' size='340' side='right'caption='[[3ga5]], [[Resolution|resolution]] 1.87Å' scene=''> | | <StructureSection load='3ga5' size='340' side='right'caption='[[3ga5]], [[Resolution|resolution]] 1.87Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ga5]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GA5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3GA5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3ga5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GA5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GA5 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=RGG:(2R)-2,3-DIHYDROXYPROPYL+BETA-D-GALACTOPYRANOSIDE'>RGG</scene>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.87Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gca|1gca]], [[1gcg|1gcg]], [[3gbp|3gbp]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=RGG:(2R)-2,3-DIHYDROXYPROPYL+BETA-D-GALACTOPYRANOSIDE'>RGG</scene>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3ga5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ga5 OCA], [http://pdbe.org/3ga5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ga5 RCSB], [http://www.ebi.ac.uk/pdbsum/3ga5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ga5 ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ga5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ga5 OCA], [https://pdbe.org/3ga5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ga5 RCSB], [https://www.ebi.ac.uk/pdbsum/3ga5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ga5 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DGAL_SALTY DGAL_SALTY]] 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. | + | [https://www.uniprot.org/uniprot/MGLB_SALTY MGLB_SALTY] Part of the ABC transporter complex MglABC involved in galactose/methyl galactoside import (By similarity). In addition, binds D-galactose and D-glucose and plays a role in the chemotaxis towards these two sugars by interacting with the Trg chemoreceptor (Probable).[UniProtKB:P0AEE5]<ref>PMID:8132630</ref> <ref>PMID:8240551</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Mowbray, S L]]
| + | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium]] |
| - | [[Category: Sooriyaarachchi, S]]
| + | [[Category: Mowbray SL]] |
| - | [[Category: Ubhayasekera, W]]
| + | [[Category: Sooriyaarachchi S]] |
| - | [[Category: Calcium]]
| + | [[Category: Ubhayasekera W]] |
| - | [[Category: Chemotaxis]]
| + | |
| - | [[Category: Glucose/galactose binding protein]]
| + | |
| - | [[Category: Glyceryl galactoside]]
| + | |
| - | [[Category: Periplasm]]
| + | |
| - | [[Category: Salmonella enterica serovar typhimurium]] | + | |
| - | [[Category: Sugar binding protein]] | + | |
| - | [[Category: Sugar transport]] | + | |
| - | [[Category: Transport]] | + | |
| Structural highlights
Function
MGLB_SALTY Part of the ABC transporter complex MglABC involved in galactose/methyl galactoside import (By similarity). In addition, binds D-galactose and D-glucose and plays a role in the chemotaxis towards these two sugars by interacting with the Trg chemoreceptor (Probable).[UniProtKB:P0AEE5][1] [2]
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
Periplasmic binding proteins are abundant in bacteria by virtue of their essential roles as high-affinity receptors in ABC transport systems and chemotaxis. One of the best studied of these receptors is the so-called glucose/galactose-binding protein. Here, we report the X-ray structure of the Salmonella typhimurium protein bound to the physiologically relevant ligand, (2R)-glyceryl-beta-D-galactopyranoside, solved by molecular replacement, and refined to 1.87 A resolution with R and R-free values of 17% and 22%. The structure identifies three amino acid residues that are diagnostic of (2R)-glyceryl-beta-D-galactopyranoside binding (Thr110, Asp154 and Gln261), as opposed to binding to the monosaccharides glucose and galactose. These three residues are conserved in essentially all available glucose/galactose-binding protein sequences, indicating that the binding of (2R)-glyceryl-beta-D-galactopyranoside is the rule rather than the exception for receptors of this type. The role of (2R)-glyceryl-beta-D-galactopyranoside in bacterial biology is discussed. Further, comparison of the available structures provides the most complete description of the conformational changes of glucose/galactose-binding protein to date. The structures follow a smooth and continuous path from the most closed structure [that bound to (2R)-glyceryl-beta-D-galactopyranoside] to the most open (an apo structure).
X-ray structure of glucose/galactose receptor from Salmonella typhimurium in complex with the physiological ligand, (2R)-glyceryl-beta-D-galactopyranoside.,Sooriyaarachchi S, Ubhayasekera W, Boos W, Mowbray SL FEBS J. 2009 Apr;276(7):2116-24. PMID:19292879[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Flocco MM, Mowbray SL. The 1.9 A x-ray structure of a closed unliganded form of the periplasmic glucose/galactose receptor from Salmonella typhimurium. J Biol Chem. 1994 Mar 25;269(12):8931-6. PMID:8132630
- ↑ Zou JY, Flocco MM, Mowbray SL. The 1.7 A refined X-ray structure of the periplasmic glucose/galactose receptor from Salmonella typhimurium. J Mol Biol. 1993 Oct 20;233(4):739-52. PMID:8240551 doi:http://dx.doi.org/10.1006/jmbi.1993.1549
- ↑ Sooriyaarachchi S, Ubhayasekera W, Boos W, Mowbray SL. X-ray structure of glucose/galactose receptor from Salmonella typhimurium in complex with the physiological ligand, (2R)-glyceryl-beta-D-galactopyranoside. FEBS J. 2009 Apr;276(7):2116-24. PMID:19292879 doi:10.1111/j.1742-4658.2009.06945.x
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