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1fqd

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(New page: 200px<br /><applet load="1fqd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fqd, resolution 2.3&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1fqd.jpg|left|200px]]<br /><applet load="1fqd" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1fqd, resolution 2.3&Aring;" />
 
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'''CRYSTAL STRUCTURE OF MALTOTETRAITOL BOUND TO CLOSED-FORM MALTODEXTRIN BINDING PROTEIN'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF MALTOTETRAITOL BOUND TO CLOSED-FORM MALTODEXTRIN BINDING PROTEIN==
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The structure of the maltodextrin or maltose-binding protein, an initial, receptor for bacterial ABC-type active transport and chemotaxis, consists, of two globular domains that are separated by a groove wherein the ligand, is bound and enclosed by an inter-domain rotation. Here, we report the, determination of the crystal structures of the protein complexed with, reduced maltooligosaccharides (maltotriitol and maltotetraitol) in both, the "closed" and "open" forms. Although these modified sugars bind to the, receptor, they are not transported by the wild-type transporter. In the, closed structures, the reduced sugars are buried in the groove and bound, by both domains, one domain mainly by hydrogen-bonding interactions and, the other domain primarily by non-polar interactions with aromatic, side-chains. In the open structures, which abrogate both cellular, activities of active transport and chemotaxis because of the large, separation between the two domains, the sugars are bound almost, exclusively to the domain rich in aromatic residues. The binding site for, the open chain glucitol residue extends to a subsite that is distinct from, those for the glucose residues that were uncovered in prior structural, studies of the binding of active linear maltooligosaccharides. Occupation, of this subsite may also account for the inability of the reduced, oligosaccharides to be transported. The structures reported here, combined, with those previously determined for several other complexes with active, oligosaccharides in the closed form and with cyclodextrin in the open, form, revealed at least four distinct modes of ligand binding but with, only one being functionally active. This versatility reflects the, flexibility of the protein, from very large motions of interdomain, rotation to more localized side-chain conformational changes, and, adaptation by the oligosaccharides as well.
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<StructureSection load='1fqd' size='340' side='right'caption='[[1fqd]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1fqd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FQD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FQD 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]] 2.3&#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=GLO:D-GLUCOSE+IN+LINEAR+FORM'>GLO</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=1fqd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fqd OCA], [https://pdbe.org/1fqd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fqd RCSB], [https://www.ebi.ac.uk/pdbsum/1fqd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fqd 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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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fq/1fqd_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1fqd ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1FQD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FQD OCA].
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*[[Maltose-binding protein 3D structures|Maltose-binding protein 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structures of the maltodextrin/maltose-binding protein complexed with reduced oligosaccharides: flexibility of tertiary structure and ligand binding., Duan X, Hall JA, Nikaido H, Quiocho FA, J Mol Biol. 2001 Mar 9;306(5):1115-26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11237621 11237621]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Duan, X.]]
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[[Category: Duan X]]
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[[Category: Hall, J.A.]]
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[[Category: Hall JA]]
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[[Category: Nikaido, H.]]
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[[Category: Nikaido H]]
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[[Category: Quiocho, F.A.]]
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[[Category: Quiocho FA]]
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[[Category: maltotetraitol]]
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[[Category: sugar-binding protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:09:36 2007''
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Current revision

CRYSTAL STRUCTURE OF MALTOTETRAITOL BOUND TO CLOSED-FORM MALTODEXTRIN BINDING PROTEIN

PDB ID 1fqd

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