1glg: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
(7 intermediate revisions by the same user not shown)
Line 1: Line 1:
==CRYSTALLOGRAPHIC ANALYSIS OF THE EPIMERIC AND ANOMERIC SPECIFICITY OF THE PERIPLASMIC TRANSPORT(SLASH)CHEMOTACTIC PROTEIN RECEPTOR FOR D-GLUCOSE AND D-GALACTOSE==
==CRYSTALLOGRAPHIC ANALYSIS OF THE EPIMERIC AND ANOMERIC SPECIFICITY OF THE PERIPLASMIC TRANSPORT(SLASH)CHEMOTACTIC PROTEIN RECEPTOR FOR D-GLUCOSE AND D-GALACTOSE==
<StructureSection load='1glg' size='340' side='right' caption='[[1glg]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='1glg' size='340' side='right'caption='[[1glg]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1glg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. 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>
<table><tr><td colspan='2'>[[1glg]] 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=1GLG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GLG FirstGlance]. <br>
</td></tr><tr><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><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]] 2&#8491;</td></tr>
<tr><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='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=GAL:BETA-D-GALACTOSE'>GAL</scene></td></tr>
<table>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1glg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1glg OCA], [https://pdbe.org/1glg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1glg RCSB], [https://www.ebi.ac.uk/pdbsum/1glg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1glg 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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gl/1glg_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gl/1glg_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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/chain_selection.php?pdb_ID=2ata ConSurf].
</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=1glg ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The 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., &amp; 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<ref>PMID:8161535</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
== References ==
== References ==
<references/>
<references/>
Line 29: Line 25:
</StructureSection>
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Quiocho, F A.]]
[[Category: Large Structures]]
[[Category: Vyas, M N.]]
[[Category: Quiocho FA]]
[[Category: Vyas, N K.]]
[[Category: Vyas MN]]
[[Category: Galactose-binding protein]]
[[Category: Vyas NK]]

Latest revision as of 10:25, 7 February 2024

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

1glg is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

References

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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
  5. ↑ 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

1glg, resolution 2.00Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=1glg&oldid=4044259"