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| - | [[Image:2fw0.gif|left|200px]]<br /><applet load="2fw0" size="350" color="white" frame="true" align="right" spinBox="true" | |
| - | caption="2fw0, resolution 1.55Å" /> | |
| - | '''Apo Open Form of Glucose/Galactose Binding Protein'''<br /> | |
| | | | |
| - | ==Overview== | + | ==Apo Open Form of Glucose/Galactose Binding Protein== |
| - | 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. | + | <StructureSection load='2fw0' size='340' side='right'caption='[[2fw0]], [[Resolution|resolution]] 1.55Å' scene=''> |
| | + | == Structural highlights == |
| | + | <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='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='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='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> |
| | + | </table> |
| | + | == Function == |
| | + | [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 == |
| | + | [[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/fw/2fw0_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=2fw0 ConSurf]. |
| | + | <div style="clear:both"></div> |
| | + | <div style="background-color:#fffaf0;"> |
| | + | == 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. |
| | | | |
| - | ==About this Structure==
| + | 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<ref>PMID:17473016</ref> |
| - | 2FW0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=CIT:'>CIT</scene> and <scene name='pdbligand=MLA:'>MLA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FW0 OCA].
| + | |
| | | | |
| - | ==Reference==
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17473016 17473016]
| + | </div> |
| | + | <div class="pdbe-citations 2fw0" style="background-color:#fffaf0;"></div> |
| | + | == References == |
| | + | <references/> |
| | + | __TOC__ |
| | + | </StructureSection> |
| | [[Category: Escherichia coli]] | | [[Category: Escherichia coli]] |
| - | [[Category: Single protein]] | + | [[Category: Large Structures]] |
| - | [[Category: Borrok, M.J.]] | + | [[Category: Borrok MJ]] |
| - | [[Category: Forest, K.T.]] | + | [[Category: Forest KT]] |
| - | [[Category: Kiessling, L.L.]] | + | [[Category: Kiessling LL]] |
| - | [[Category: CA]]
| + | |
| - | [[Category: CIT]]
| + | |
| - | [[Category: MLA]]
| + | |
| - | [[Category: NA]]
| + | |
| - | [[Category: chemotaxis]]
| + | |
| - | [[Category: ggbp]]
| + | |
| - | [[Category: hinge]]
| + | |
| - | [[Category: periplasmic binding protein]]
| + | |
| - | [[Category: transport]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 13:55:47 2008''
| + | |
| 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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