1dmb

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(New page: 200px<br /><applet load="1dmb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dmb, resolution 1.8&Aring;" /> '''REFINED 1.8 ANGSTROMS...)
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[[Image:1dmb.gif|left|200px]]<br /><applet load="1dmb" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1dmb, resolution 1.8&Aring;" />
 
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'''REFINED 1.8 ANGSTROMS STRUCTURE REVEALS THE MECHANISM OF BINDING OF A CYCLIC SUGAR, BETA-CYCLODEXTRIN, TO THE MALTODEXTRIN BINDING PROTEIN'''<br />
 
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==Overview==
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==REFINED 1.8 ANGSTROMS STRUCTURE REVEALS THE MECHANISM OF BINDING OF A CYCLIC SUGAR, BETA-CYCLODEXTRIN, TO THE MALTODEXTRIN BINDING PROTEIN==
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The maltodextrin binding protein from Escherichia coli serves as the, initial receptor for both the active transport of and chemotaxis toward a, range of linear maltose sugars. The X-ray structures of both the, maltose-bound and sugar-free forms of the protein have been previously, described [Spurlino, J. C., Lu, G.-Y., &amp; Quiocho, F. A. (1991) J. Biol., Chem. 266, 5202-5219; Sharff, A. J., Rodseth, L. E., Spurlino, J. C., &amp;, Quocho, F. A. (1992) Biochemistry 31, 10657-10663]. The X-ray crystal, structure of the maltodextrin binding protein complexed with, cyclomaltoheptaose (beta-cyclodextrin) has been determined from a single, crystal. The structure has been refined to a final R-value of 21% at 1.8-A, resolution. Although not a physiological ligand for the maltodextrin, binding protein, beta-cyclodextrin has been shown to bind with a Kd of the, same order as those of the linear maltodextrin substrates. The observed, structure shows that the complexed protein remains in the fully open, conformation and is almost identical to the structure of the unliganded, protein. The sugar sits in the open cleft with three glucosyl units bound, to the C-domain at the base of the cleft, in a similar position to, maltotriose, the most tightly bound ligand. The top of the ring is loosely, bound to the upper edge of the cleft on the N-domain. The sugar makes a, total of 94 productive interactions (of less than 4.0-A length) with the, protein and with bound water molecules.(ABSTRACT TRUNCATED AT 250 WORDS)
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<StructureSection load='1dmb' size='340' side='right'caption='[[1dmb]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1dmb]] 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=1DMB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DMB 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]] 1.8&#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=PRD_900012:beta-cyclodextrin'>PRD_900012</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=1dmb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dmb OCA], [https://pdbe.org/1dmb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dmb RCSB], [https://www.ebi.ac.uk/pdbsum/1dmb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dmb 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/dm/1dmb_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=1dmb 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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1DMB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with BCD as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DMB 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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Refined 1.8-A structure reveals the mode of binding of beta-cyclodextrin to the maltodextrin binding protein., Sharff AJ, Rodseth LE, Quiocho FA, Biochemistry. 1993 Oct 12;32(40):10553-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8399200 8399200]
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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: Quiocho, F.A.]]
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[[Category: Quiocho FA]]
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[[Category: Sharff, A.J.]]
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[[Category: Sharff AJ]]
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[[Category: BCD]]
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[[Category: sugar transport]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:24:19 2007''
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Current revision

REFINED 1.8 ANGSTROMS STRUCTURE REVEALS THE MECHANISM OF BINDING OF A CYCLIC SUGAR, BETA-CYCLODEXTRIN, TO THE MALTODEXTRIN BINDING PROTEIN

PDB ID 1dmb

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