3puw

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<StructureSection load='3puw' size='340' side='right'caption='[[3puw]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='3puw' size='340' side='right'caption='[[3puw]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3puw]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PUW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PUW FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3puw]] 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=3PUW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PUW 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=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=UMQ:UNDECYL-MALTOSIDE'>UMQ</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]] 2.3&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3puv|3puv]], [[3pux|3pux]], [[3puy|3puy]], [[3puz|3puz]], [[3pv0|3pv0]], [[3rlf|3rlf]]</div></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=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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>, <scene name='pdbligand=UMQ:UNDECYL-MALTOSIDE'>UMQ</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b4034, ECDH10B_4223, JW3994, malE ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), b4033, ECDH10B_4222, JW3993, malF ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), b4032, ECDH10B_4221, JW3992, malG ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), b4035, ECDH10B_4224, JW3995, malK ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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/Maltose-transporting_ATPase Maltose-transporting ATPase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.19 3.6.3.19] </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=3puw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3puw OCA], [https://pdbe.org/3puw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3puw RCSB], [https://www.ebi.ac.uk/pdbsum/3puw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3puw 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=3puw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3puw OCA], [https://pdbe.org/3puw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3puw RCSB], [https://www.ebi.ac.uk/pdbsum/3puw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3puw ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/MALK_ECOLI MALK_ECOLI]] Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Responsible for energy coupling to the transport system. [[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. [[https://www.uniprot.org/uniprot/MALG_ECOLI MALG_ECOLI]] Part of the binding-protein-dependent transport system for maltose; probably responsible for the translocation of the substrate across the membrane. [[https://www.uniprot.org/uniprot/MALF_ECOLI MALF_ECOLI]] Part of the binding-protein-dependent transport system for maltose; probably responsible for the translocation of the substrate across the membrane.
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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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ATP-binding cassette transporters are powered by ATP, but the mechanism by which these transporters hydrolyze ATP is unclear. In this study, four crystal structures of the full-length wild-type maltose transporter, stabilized by adenosine 5'-(beta,gamma-imido)triphosphate or ADP in conjunction with phosphate analogs , , or , were determined to 2.2- to 2.4-A resolution. These structures led to the assignment of two enzymatic states during ATP hydrolysis and demonstrate specific functional roles of highly conserved residues in the nucleotide-binding domain, suggesting that ATP-binding cassette transporters catalyze ATP hydrolysis via a general base mechanism.
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Snapshots of the maltose transporter during ATP hydrolysis.,Oldham ML, Chen J Proc Natl Acad Sci U S A. 2011 Aug 8. PMID:21825153<ref>PMID:21825153</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 3puw" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Maltose-binding protein 3D structures|Maltose-binding protein 3D structures]]
*[[Maltose-binding protein 3D structures|Maltose-binding protein 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Ecoli]]
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[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Maltose-transporting ATPase]]
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[[Category: Chen J]]
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[[Category: Chen, J]]
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[[Category: Oldham ML]]
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[[Category: Oldham, M L]]
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[[Category: Abc transporter importer atpase]]
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[[Category: Atp binding cassette nucleotide binding domain substrate binding protein transmembrane domain]]
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[[Category: Atp binding maltodextrin binding]]
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[[Category: Hydrolase-transport protein complex]]
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[[Category: Transmembrane integral membrane]]
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Current revision

Crystal Structure of an outward-facing MBP-Maltose transporter complex bound to ADP-AlF4

PDB ID 3puw

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