1gcg

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Current revision (07:24, 7 February 2024) (edit) (undo)
 
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<StructureSection load='1gcg' size='340' side='right'caption='[[1gcg]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='1gcg' size='340' side='right'caption='[[1gcg]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1gcg]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GCG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GCG FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1gcg]] is a 1 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=1GCG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GCG FirstGlance]. <br>
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</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></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=1gcg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gcg OCA], [https://pdbe.org/1gcg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gcg RCSB], [https://www.ebi.ac.uk/pdbsum/1gcg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gcg 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=1gcg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gcg OCA], [https://pdbe.org/1gcg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gcg RCSB], [https://www.ebi.ac.uk/pdbsum/1gcg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gcg ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://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.
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[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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</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=1gcg 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=1gcg ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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The three-dimensional structure of a ligand-free closed form of the glucose/galactose binding protein from Salmonella typhimurium has been determined at a resolution of 1.9 A. The crystallographic R-factor for the refined structure is 17.9%. The model contains all the atoms of the 309 residues of the protein sequence, a calcium ion, and 174 water molecules. The root mean square (r.m.s.) deviations for the whole molecule are: 0.010 A for bond lengths and 2.44 degrees for bond angles, indicating a good stereochemistry for the model. This structure shows that the protein is able to close in the absence of ligand, adopting a conformation similar to the liganded form but slightly more open. Water molecules satisfy the hydrogen bonding ability of the hydrophilic side chains of the binding site in a manner which is reminiscent of the sugars' hydrogen-bonding patterns. Since packing forces are weak, the crystallization event is unlikely to trigger a change from an open to a closed conformation. Instead, the latter must be one of the species in equilibrium in solution which is selected by packing in the crystal lattice.
 
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The 1.9 A x-ray structure of a closed unliganded form of the periplasmic glucose/galactose receptor from Salmonella typhimurium.,Flocco MM, Mowbray SL J Biol Chem. 1994 Mar 25;269(12):8931-6. PMID:8132630<ref>PMID:8132630</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1gcg" style="background-color:#fffaf0;"></div>
 
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Flocco, M M]]
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[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
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[[Category: Mowbray, S L]]
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[[Category: Flocco MM]]
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[[Category: Galactose-binding protein]]
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[[Category: Mowbray SL]]

Current revision

THE 1.9 ANGSTROMS X-RAY STRUCTURE OF A CLOSED UNLIGANDED FORM OF THE PERIPLASMIC GLUCOSE(SLASH)GALACTOSE RECEPTOR FROM SALMONELLA TYPHIMURIUM

PDB ID 1gcg

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