1gcg: Difference between revisions
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<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=1gcg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gcg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1gcg RCSB], [http://www.ebi.ac.uk/pdbsum/1gcg PDBsum]</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=1gcg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gcg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1gcg RCSB], [http://www.ebi.ac.uk/pdbsum/1gcg PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== 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. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] |
Revision as of 04:10, 25 December 2014
THE 1.9 ANGSTROMS X-RAY STRUCTURE OF A CLOSED UNLIGANDED FORM OF THE PERIPLASMIC GLUCOSE(SLASH)GALACTOSE RECEPTOR FROM SALMONELLA TYPHIMURIUMTHE 1.9 ANGSTROMS X-RAY STRUCTURE OF A CLOSED UNLIGANDED FORM OF THE PERIPLASMIC GLUCOSE(SLASH)GALACTOSE RECEPTOR FROM SALMONELLA TYPHIMURIUM
Structural highlights
Function[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. 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 PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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