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| ==Apo Open Form of Glucose/Galactose Binding Protein== | | ==Apo Open Form of Glucose/Galactose Binding Protein== |
- | <StructureSection load='2fw0' size='340' side='right' caption='[[2fw0]], [[Resolution|resolution]] 1.55Å' scene=''> | + | <StructureSection load='2fw0' size='340' side='right'caption='[[2fw0]], [[Resolution|resolution]] 1.55Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[2fw0]] 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=2FW0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FW0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2fw0]] 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=2FW0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FW0 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=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=MLA:MALONIC+ACID'>MLA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 1.55Å</td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2gbp|2gbp]], [[1gcg|1gcg]], [[1glg|1glg]]</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=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=MLA:MALONIC+ACID'>MLA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mglB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=2fw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fw0 OCA], [https://pdbe.org/2fw0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fw0 RCSB], [https://www.ebi.ac.uk/pdbsum/2fw0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fw0 ProSAT]</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=2fw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fw0 OCA], [http://pdbe.org/2fw0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fw0 RCSB], [http://www.ebi.ac.uk/pdbsum/2fw0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2fw0 ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/DGAL_ECOLI 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. | + | [https://www.uniprot.org/uniprot/MGLB_ECOLI MGLB_ECOLI] Part of the ABC transporter complex MglABC involved in galactose/methyl galactoside import (Probable). 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 (PubMed:3057628, PubMed:4927373). Chemotaxis requires MglB, but not MglA or MglC (PubMed:6294056).<ref>PMID:3057628</ref> <ref>PMID:4927373</ref> <ref>PMID:6294056</ref> <ref>PMID:1719366</ref> <ref>PMID:6294056</ref> |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
- | [[Category: Borrok, M J]] | + | [[Category: Large Structures]] |
- | [[Category: Forest, K T]] | + | [[Category: Borrok MJ]] |
- | [[Category: Kiessling, L L]] | + | [[Category: Forest KT]] |
- | [[Category: Chemotaxis]] | + | [[Category: Kiessling LL]] |
- | [[Category: Ggbp]]
| + | |
- | [[Category: Hinge]]
| + | |
- | [[Category: Periplasmic binding protein]]
| + | |
- | [[Category: Transport]]
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- | [[Category: Transport protein]]
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| Structural highlights
Function
MGLB_ECOLI Part of the ABC transporter complex MglABC involved in galactose/methyl galactoside import (Probable). 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 (PubMed:3057628, PubMed:4927373). Chemotaxis requires MglB, but not MglA or MglC (PubMed:6294056).[1] [2] [3] [4] [5]
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
D-Glucose/D-Galactose-binding protein (GGBP) mediates chemotaxis toward and active transport of glucose and galactose in a number of bacterial species. GGBP, like other periplasmic binding proteins, can exist in open (ligand-free) and closed (ligand-bound) states. We report a 0.92 angstroms resolution structure of GGBP from Escherichia coli in the glucose-bound state and the first structure of an open, unbound form of GGBP (at 1.55 angstroms resolution). These structures vary in the angle between the two structural domains; the observed difference of 31 degrees arises from torsion angle changes in a three-segment hinge. A comparison with the closely related periplasmic receptors, ribose- and allose-binding proteins, shows that the GGBP hinge residue positions that undergo the largest conformational changes are different. Furthermore, the high-quality data collected for the atomic resolution glucose-bound structure allow for the refinement of specific hydrogen atom positions, the assignment of alternate side chain conformations, the first description of CO(2) trapped after radiation-induced decarboxylation, and insight into the role of the exo-anomeric effect in sugar binding. Together, these structures provide insight into how the hinge-bending movement of GGBP facilitates ligand binding, transport, and signaling.
Conformational changes of glucose/galactose-binding protein illuminated by open, unliganded, and ultra-high-resolution ligand-bound structures.,Borrok MJ, Kiessling LL, Forest KT Protein Sci. 2007 Jun;16(6):1032-41. Epub 2007 May 1. PMID:17473016[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Vyas NK, Vyas MN, Quiocho FA. Sugar and signal-transducer binding sites of the Escherichia coli galactose chemoreceptor protein. Science. 1988 Dec 2;242(4883):1290-5. PMID:3057628
- ↑ Hazelbauer GL, Adler J. Role of the galactose binding protein in chemotaxis of Escherichia coli toward galactose. Nat New Biol. 1971 Mar 24;230(12):101-4. PMID:4927373 doi:10.1038/newbio230101a0
- ↑ Harayama S, Bollinger J, Iino T, Hazelbauer GL. Characterization of the mgl operon of Escherichia coli by transposon mutagenesis and molecular cloning. J Bacteriol. 1983 Jan;153(1):408-15. PMID:6294056 doi:10.1128/jb.153.1.408-415.1983
- ↑ Hogg RW, Voelker C, Von Carlowitz I. Nucleotide sequence and analysis of the mgl operon of Escherichia coli K12. Mol Gen Genet. 1991 Oct;229(3):453-9. PMID:1719366 doi:10.1007/BF00267469
- ↑ Harayama S, Bollinger J, Iino T, Hazelbauer GL. Characterization of the mgl operon of Escherichia coli by transposon mutagenesis and molecular cloning. J Bacteriol. 1983 Jan;153(1):408-15. PMID:6294056 doi:10.1128/jb.153.1.408-415.1983
- ↑ Borrok MJ, Kiessling LL, Forest KT. Conformational changes of glucose/galactose-binding protein illuminated by open, unliganded, and ultra-high-resolution ligand-bound structures. Protein Sci. 2007 Jun;16(6):1032-41. Epub 2007 May 1. PMID:17473016 doi:http://dx.doi.org/10.1110/ps.062707807
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