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| | <StructureSection load='5iws' size='340' side='right'caption='[[5iws]], [[Resolution|resolution]] 2.55Å' scene=''> | | <StructureSection load='5iws' size='340' side='right'caption='[[5iws]], [[Resolution|resolution]] 2.55Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5iws]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Baccz Baccz]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IWS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IWS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5iws]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus_E33L Bacillus cereus E33L]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IWS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IWS FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MAL:MALTOSE'>MAL</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]] 2.551Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ptsG, BCE33L0344 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=288681 BACCZ])</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=5iws FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5iws OCA], [https://pdbe.org/5iws PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5iws RCSB], [https://www.ebi.ac.uk/pdbsum/5iws PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5iws ProSAT]</span></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='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=5iws FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5iws OCA], [http://pdbe.org/5iws PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5iws RCSB], [http://www.ebi.ac.uk/pdbsum/5iws PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5iws ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/Q63GK8_BACCZ Q63GK8_BACCZ]] 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.[SAAS:SAAS00547063] | + | [https://www.uniprot.org/uniprot/Q63GK8_BACCZ Q63GK8_BACCZ] 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.[SAAS:SAAS00547063] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Baccz]] | + | [[Category: Bacillus cereus E33L]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Levin, E J]] | + | [[Category: Levin EJ]] |
| - | [[Category: McCoy, J G]] | + | [[Category: McCoy JG]] |
| - | [[Category: NYCOMPS, New York Consortium on Membrane Protein Structure]]
| + | [[Category: Ren Z]] |
| - | [[Category: Ren, Z]] | + | [[Category: Zhou M]] |
| - | [[Category: Zhou, M]] | + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: New york consortium on membrane protein structure]]
| + | |
| - | [[Category: Nycomp]]
| + | |
| - | [[Category: Psi-biology]]
| + | |
| - | [[Category: Structural genomic]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Transporter]]
| + | |
| Structural highlights
Function
Q63GK8_BACCZ 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.[SAAS:SAAS00547063]
Publication Abstract from PubMed
The phosphoenolpyruvate:carbohydrate phosphotransferase systems are found in bacteria, where they play central roles in sugar uptake and regulation of cellular uptake processes. Little is known about how the membrane-embedded components (EIICs) selectively mediate the passage of carbohydrates across the membrane. Here we report the functional characterization and 2.55-A resolution structure of a maltose transporter, bcMalT, belonging to the glucose superfamily of EIIC transporters. bcMalT crystallized in an outward-facing occluded conformation, in contrast to the structure of another glucose superfamily EIIC, bcChbC, which crystallized in an inward-facing occluded conformation. The structures differ in the position of a structurally conserved substrate-binding domain that is suggested to play a central role in sugar transport. In addition, molecular dynamics simulations suggest a potential pathway for substrate entry from the periplasm into the bcMalT substrate-binding site. These results provide a mechanistic framework for understanding substrate recognition and translocation for the glucose superfamily EIIC transporters.
The Structure of a Sugar Transporter of the Glucose EIIC Superfamily Provides Insight into the Elevator Mechanism of Membrane Transport.,McCoy JG, Ren Z, Stanevich V, Lee J, Mitra S, Levin EJ, Poget S, Quick M, Im W, Zhou M Structure. 2016 May 3. pii: S0969-2126(16)30039-9. doi:, 10.1016/j.str.2016.04.003. PMID:27161976[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ McCoy JG, Ren Z, Stanevich V, Lee J, Mitra S, Levin EJ, Poget S, Quick M, Im W, Zhou M. The Structure of a Sugar Transporter of the Glucose EIIC Superfamily Provides Insight into the Elevator Mechanism of Membrane Transport. Structure. 2016 May 3. pii: S0969-2126(16)30039-9. doi:, 10.1016/j.str.2016.04.003. PMID:27161976 doi:http://dx.doi.org/10.1016/j.str.2016.04.003
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