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| | ==IIAGLC-ZN COMPLEX== | | ==IIAGLC-ZN COMPLEX== |
| - | <StructureSection load='1f3z' size='340' side='right' caption='[[1f3z]], [[Resolution|resolution]] 1.98Å' scene=''> | + | <StructureSection load='1f3z' size='340' side='right'caption='[[1f3z]], [[Resolution|resolution]] 1.98Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1f3z]] 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=1F3Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F3Z FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1f3z]] 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=1F3Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F3Z FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.98Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-N(pi)-phosphohistidine--sugar_phosphotransferase Protein-N(pi)-phosphohistidine--sugar phosphotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.69 2.7.1.69] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1f3z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f3z OCA], [http://pdbe.org/1f3z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1f3z RCSB], [http://www.ebi.ac.uk/pdbsum/1f3z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1f3z 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=1f3z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f3z OCA], [https://pdbe.org/1f3z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f3z RCSB], [https://www.ebi.ac.uk/pdbsum/1f3z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f3z ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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. | + | [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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Escherichia coli]] | | [[Category: Escherichia coli]] |
| - | [[Category: Comolli, L]] | + | [[Category: Large Structures]] |
| - | [[Category: Feese, M]] | + | [[Category: Comolli L]] |
| - | [[Category: Meadow, N]] | + | [[Category: Feese M]] |
| - | [[Category: Remington, S J]] | + | [[Category: Meadow N]] |
| - | [[Category: Roseman, S]] | + | [[Category: Remington SJ]] |
| - | [[Category: Phosphotransferase]]
| + | [[Category: Roseman S]] |
| - | [[Category: Signal transduction]]
| + | |
| - | [[Category: Sugar transport]]
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| Structural highlights
Function
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
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
In Escherichia coli, the glucose-specific phosphocarrier protein of the phosphotransferase system (PTS), IIAGlc (IIIGlc in older literature), is also the central regulatory protein of the PTS. Depending upon its state of phosphorylation, IIAGlc binds to a number of different proteins that display no apparent sequence homology. Previous structural studies suggested that nonspecific hydrophobic interactions, specific salt bridges, and an intermolecular Zn(II) binding site contribute to the wide latitude in IIAGlc binding sites. Two new crystal forms of IIAGlc have been solved at high resolution, and the models were compared to those previously studied. The major intermolecular contacts in the crystals differ in detail, but all involve the hydrophobic active site of IIAGlc interacting with a hydrophobic patch on a neighbor and all are shown to be surprisingly similar to the physiologically relevant regulatory interaction of IIAGlc with glycerol kinase. In two crystal forms, a helix on one molecule interacts with the face of another, while in the other crystal form, the primary crystal contact consists of a strand of beta-sheet that contributes to an intermolecular Zn(II) binding site with tetrahedral ligation identical to that of the zinc peptidase thermolysin. Thus, relatively nonspecific hydrophobic interactions combined with specific salt bridges and an intermolecular cation binding site (cation-promoted association) permit a regulatory protein to bind to target proteins that have little or no sequence or structural homology with one another. It is suggested that signal transduction by IIAGlc is a binary switch in which phosphorylation at the active site directly controls binding to target molecules.
Structural studies of the Escherichia coli signal transducing protein IIAGlc: implications for target recognition.,Feese MD, Comolli L, Meadow ND, Roseman S, Remington SJ Biochemistry. 1997 Dec 23;36(51):16087-96. PMID:9405042[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Feese MD, Comolli L, Meadow ND, Roseman S, Remington SJ. Structural studies of the Escherichia coli signal transducing protein IIAGlc: implications for target recognition. Biochemistry. 1997 Dec 23;36(51):16087-96. PMID:9405042 doi:10.1021/bi971999e
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