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3pv0

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'''Unreleased structure'''
 
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The entry 3pv0 is ON HOLD until Paper Publication
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==Crystal Structure of a pre-translocation state MBP-Maltose transporter complex without nucleotide==
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<StructureSection load='3pv0' size='340' side='right'caption='[[3pv0]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3pv0]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PV0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PV0 FirstGlance]. <br>
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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]] 3.1&#8491;</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=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PGV:(1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL+(11E)-OCTADEC-11-ENOATE'>PGV</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</scene></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=3pv0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pv0 OCA], [https://pdbe.org/3pv0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pv0 RCSB], [https://www.ebi.ac.uk/pdbsum/3pv0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pv0 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Adenosine triphosphate (ATP)-binding cassette (ABC) transporters convert chemical energy from ATP hydrolysis to mechanical work for substrate translocation. They function by alternating between two states, exposing the substrate-binding site to either side of the membrane. A key question that remains to be addressed is how substrates initiate the transport cycle. Using x-ray crystallography, we have captured the maltose transporter in an intermediate step between the inward- and outward-facing states. We show that interactions with substrate-loaded maltose-binding protein in the periplasm induce a partial closure of the MalK dimer in the cytoplasm. ATP binding to this conformation then promotes progression to the outward-facing state. These results, interpreted in light of biochemical and functional studies, provide a structural basis to understand allosteric communication in ABC transporters.
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Authors: Oldham, M.L., Chen, J.
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Crystal structure of the maltose transporter in a pretranslocation intermediate state.,Oldham ML, Chen J Science. 2011 Jun 3;332(6034):1202-5. Epub 2011 May 12. PMID:21566157<ref>PMID:21566157</ref>
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Description: Crystal Structure of a pre-translocation state MBP-Maltose transporter complex without nucleotide
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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 3pv0" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Maltose-binding protein 3D structures|Maltose-binding protein 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli K-12]]
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[[Category: Large Structures]]
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[[Category: Chen J]]
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[[Category: Oldham ML]]

Current revision

Crystal Structure of a pre-translocation state MBP-Maltose transporter complex without nucleotide

PDB ID 3pv0

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