3pux
From Proteopedia
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- | [[ | + | ==Crystal Structure of an outward-facing MBP-Maltose transporter complex bound to ADP-BeF3== |
+ | <StructureSection load='3pux' size='340' side='right' caption='[[3pux]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[3pux]] is a 5 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=3PUX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PUX FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=MAL:MALTOSE'>MAL</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> | ||
+ | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3puv|3puv]], [[3puw|3puw]], [[3puy|3puy]], [[3puz|3puz]], [[3pv0|3pv0]], [[3rlf|3rlf]]</td></tr> | ||
+ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b4034, ECDH10B_4223, JW3994, malE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]), b4033, ECDH10B_4222, JW3993, malF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]), b4032, ECDH10B_4221, JW3992, malG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]), b4035, ECDH10B_4224, JW3995, malK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr> | ||
+ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Maltose-transporting_ATPase Maltose-transporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.19 3.6.3.19] </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=3pux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pux OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3pux RCSB], [http://www.ebi.ac.uk/pdbsum/3pux PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | 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. | ||
- | + | 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> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
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- | + | ||
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- | + | ||
==See Also== | ==See Also== | ||
+ | *[[ABC transporter|ABC transporter]] | ||
*[[Maltose-binding protein|Maltose-binding protein]] | *[[Maltose-binding protein|Maltose-binding protein]] | ||
- | + | == References == | |
- | == | + | <references/> |
- | < | + | __TOC__ |
+ | </StructureSection> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Maltose-transporting ATPase]] | [[Category: Maltose-transporting ATPase]] | ||
- | [[Category: Chen, J | + | [[Category: Chen, J]] |
- | [[Category: Oldham, M L | + | [[Category: Oldham, M L]] |
[[Category: Abc transporter]] | [[Category: Abc transporter]] | ||
[[Category: Atp binding]] | [[Category: Atp binding]] |
Revision as of 12:30, 9 December 2014
Crystal Structure of an outward-facing MBP-Maltose transporter complex bound to ADP-BeF3
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Categories: Escherichia coli | Maltose-transporting ATPase | Chen, J | Oldham, M L | Abc transporter | Atp binding | Atp binding cassette | Atpase | Hydrolase-transport protein complex | Importer | Maltodextrin binding | Nucleotide binding domain | Substrate binding protein | Transmembrane integral membrane