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3fh6
From Proteopedia
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| - | {{Seed}} | ||
| - | [[Image:3fh6.png|left|200px]] | ||
| - | < | + | ==Crystal structure of the resting state maltose transporter from E. coli== |
| - | + | <StructureSection load='3fh6' size='340' side='right'caption='[[3fh6]], [[Resolution|resolution]] 4.50Å' scene=''> | |
| - | You may | + | == Structural highlights == |
| - | + | <table><tr><td colspan='2'>[[3fh6]] is a 8 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=3FH6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FH6 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4.5Å</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=3fh6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fh6 OCA], [https://pdbe.org/3fh6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fh6 RCSB], [https://www.ebi.ac.uk/pdbsum/3fh6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fh6 ProSAT]</span></td></tr> |
| - | + | </table> | |
| + | == Function == | ||
| + | [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. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fh/3fh6_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3fh6 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | ATP-binding cassette transporters couple ATP hydrolysis to substrate translocation through an alternating access mechanism, but the nature of the conformational changes in a transport cycle remains elusive. Previously we reported the structure of the maltose transporter MalFGK(2) in an outward-facing conformation in which the transmembrane (TM) helices outline a substrate-binding pocket open toward the periplasmic surface and ATP is poised for hydrolysis along the closed nucleotide-binding dimer interface. Here we report the structure of the nucleotide-free maltose transporter in which the substrate binding pocket is only accessible from the cytoplasm and the nucleotide-binding interface is open. Comparison of the same transporter crystallized in two different conformations reveals that alternating access involves rigid-body rotations of the TM subdomains that are coupled to the closure and opening of the nucleotide-binding domain interface. The comparison also reveals that point mutations enabling binding protein-independent transport line dynamic interfaces in the TM region. | ||
| - | + | Alternating access in maltose transporter mediated by rigid-body rotations.,Khare D, Oldham ML, Orelle C, Davidson AL, Chen J Mol Cell. 2009 Feb 27;33(4):528-36. PMID:19250913<ref>PMID:19250913</ref> | |
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 3fh6" style="background-color:#fffaf0;"></div> | ||
| - | + | ==See Also== | |
| - | + | *[[Maltose-binding protein 3D structures|Maltose-binding protein 3D structures]] | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | == | + | [[Category: Escherichia coli K-12]] |
| - | + | [[Category: Large Structures]] | |
| - | + | [[Category: Chen J]] | |
| - | == | + | [[Category: Davidson AL]] |
| - | < | + | [[Category: Khare D]] |
| - | [[Category: Escherichia coli | + | [[Category: Oldham ML]] |
| - | [[Category: | + | [[Category: Orelle C]] |
| - | [[Category: Chen | + | |
| - | [[Category: Davidson | + | |
| - | [[Category: Khare | + | |
| - | [[Category: Oldham | + | |
| - | [[Category: Orelle | + | |
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Current revision
Crystal structure of the resting state maltose transporter from E. coli
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