3qnq

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<StructureSection load='3qnq' size='340' side='right'caption='[[3qnq]], [[Resolution|resolution]] 3.29&Aring;' scene=''>
<StructureSection load='3qnq' size='340' side='right'caption='[[3qnq]], [[Resolution|resolution]] 3.29&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3qnq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacc1 Bacc1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QNQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QNQ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3qnq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus_ATCC_10987 Bacillus cereus ATCC 10987]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QNQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QNQ 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=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=ZDM:NONYL+4-O-ALPHA-D-GLUCOPYRANOSYL-BETA-D-GLUCOPYRANOSIDE'>ZDM</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 3.295&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BCE_5325, celB, ChbC ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=222523 BACC1])</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=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</scene>, <scene name='pdbligand=ZDM:NONYL+4-O-ALPHA-D-GLUCOPYRANOSYL-BETA-D-GLUCOPYRANOSIDE'>ZDM</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Protein-N(pi)-phosphohistidine--sugar_phosphotransferase Protein-N(pi)-phosphohistidine--sugar phosphotransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.69 2.7.1.69] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3qnq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qnq OCA], [https://pdbe.org/3qnq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qnq RCSB], [https://www.ebi.ac.uk/pdbsum/3qnq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qnq 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=3qnq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qnq OCA], [https://pdbe.org/3qnq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qnq RCSB], [https://www.ebi.ac.uk/pdbsum/3qnq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qnq ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q72XQ0_BACC1 Q72XQ0_BACC1]
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Saccharides have a central role in the nutrition of all living organisms. Whereas several saccharide uptake systems are shared between the different phylogenetic kingdoms, the phosphoenolpyruvate-dependent phosphotransferase system exists almost exclusively in bacteria. This multi-component system includes an integral membrane protein EIIC that transports saccharides and assists in their phosphorylation. Here we present the crystal structure of an EIIC from Bacillus cereus that transports diacetylchitobiose. The EIIC is a homodimer, with an expansive interface formed between the amino-terminal halves of the two protomers. The carboxy-terminal half of each protomer has a large binding pocket that contains a diacetylchitobiose, which is occluded from both sides of the membrane with its site of phosphorylation near the conserved His250 and Glu334 residues. The structure shows the architecture of this important class of transporters, identifies the determinants of substrate binding and phosphorylation, and provides a framework for understanding the mechanism of sugar translocation.
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Crystal structure of a phosphorylation-coupled saccharide transporter.,Cao Y, Jin X, Levin EJ, Huang H, Zong Y, Quick M, Weng J, Pan Y, Love J, Punta M, Rost B, Hendrickson WA, Javitch JA, Rajashankar KR, Zhou M Nature. 2011 May 5;473(7345):50-4. Epub 2011 Apr 6. PMID:21471968<ref>PMID:21471968</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 3qnq" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacc1]]
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[[Category: Bacillus cereus ATCC 10987]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Cao, Y]]
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[[Category: Cao Y]]
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[[Category: Huang, H]]
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[[Category: Huang H]]
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[[Category: Jin, X]]
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[[Category: Jin X]]
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[[Category: Levin, E J]]
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[[Category: Levin EJ]]
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[[Category: NYCOMPS, New York Consortium on Membrane Protein Structure]]
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[[Category: Zhou M]]
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[[Category: Zhou, M]]
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[[Category: Enzyme iic]]
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[[Category: Hydrolase]]
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[[Category: Membrane protein]]
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[[Category: New york consortium on membrane protein structure]]
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[[Category: Nycomp]]
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[[Category: Phosphoenolpyruvate-sugar phosphotransferase system]]
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[[Category: Psi-biology]]
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[[Category: Structural genomic]]
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[[Category: Transport protein]]
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[[Category: Transporter]]
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Current revision

Crystal structure of the transporter ChbC, the IIC component from the N,N'-diacetylchitobiose-specific phosphotransferase system

PDB ID 3qnq

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