1gla: Difference between revisions

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-[[Image:1gla.gif|left|200px]]
-<!--
+==STRUCTURE OF THE REGULATORY COMPLEX OF ESCHERICHIA COLI IIIGLC WITH GLYCEROL KINASE==
-The line below this paragraph, containing "STRUCTURE_1gla", creates the "Structure Box" on the page.
+<StructureSection load='1gla' size='340' side='right'caption='[[1gla]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1gla]] is a 2 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=1GLA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GLA FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
-{{STRUCTURE_1gla|  PDB=1gla  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gla FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gla OCA], [https://pdbe.org/1gla PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gla RCSB], [https://www.ebi.ac.uk/pdbsum/1gla PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gla ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PTGA_ECOLI PTGA_ECOLI] The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in glucose transport.
+== 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/gl/1gla_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=1gla ConSurf].
+<div style="clear:both"></div>
-'''STRUCTURE OF THE REGULATORY COMPLEX OF ESCHERICHIA COLI IIIGLC WITH GLYCEROL KINASE'''
+==See Also==
+*[[Glycerol kinase|Glycerol kinase]]
+__TOC__
-==Overview==
+</StructureSection>
-The phosphocarrier protein IIIGlc is an integral component of the bacterial phosphotransferase (PTS) system. Unphosphorylated IIIGlc inhibits non-PTS carbohydrate transport systems by binding to diverse target proteins. The crystal structure at 2.6 A resolution of one of the targets, glycerol kinase (GK), in complex with unphosphorylated IIIGlc, glycerol, and adenosine diphosphate was determined. GK contains a region that is topologically identical to the adenosine triphosphate binding domains of hexokinase, the 70-kD heat shock cognate, and actin. IIIGlc binds far from the catalytic site of GK, indicating that long-range conformational changes mediate the inhibition of GK by IIIGlc. GK and IIIGlc are bound by hydrophobic and electrostatic interactions, with only one hydrogen bond involving an uncharged group. The phosphorylation site of IIIGlc, His90, is buried in a hydrophobic environment formed by the active site region of IIIGlc and a 3(10) helix of GK, suggesting that phosphorylation prevents IIIGlc binding to GK by directly disrupting protein-protein interactions.
-==About this Structure==
-GLA is a [[Protein complex]] structure of sequences 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=1GLA OCA].
-==Reference==
-Structure of the regulatory complex of Escherichia coli IIIGlc with glycerol kinase., Hurley JH, Faber HR, Worthylake D, Meadow ND, Roseman S, Pettigrew DW, Remington SJ, Science. 1993 Jan 29;259(5095):673-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8430315 8430315]
 [[Category: Escherichia coli]]
-[[Category: Protein complex]]
+[[Category: Large Structures]]
-[[Category: Faber, H R.]]
+[[Category: Faber HR]]
-[[Category: Hurley, J H.]]
+[[Category: Hurley JH]]
-[[Category: Meadow, N D.]]
+[[Category: Meadow ND]]
-[[Category: Pettigrew, D W.]]
+[[Category: Pettigrew DW]]
-[[Category: Remington, S J.]]
+[[Category: Remington SJ]]
-[[Category: Roseman, S.]]
+[[Category: Roseman S]]
-[[Category: Worthylake, D.]]
+[[Category: Worthylake D]]
-[[Category: Phosphotransferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 17:43:08 2008''