1omp

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(New page: 200px<br /><applet load="1omp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1omp, resolution 1.8&Aring;" /> '''CRYSTALLOGRAPHIC EVID...)
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[[Image:1omp.jpg|left|200px]]<br /><applet load="1omp" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1omp, resolution 1.8&Aring;" />
 
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'''CRYSTALLOGRAPHIC EVIDENCE OF A LARGE LIGAND-INDUCED HINGE-TWIST MOTION BETWEEN THE TWO DOMAINS OF THE MALTODEXTRIN-BINDING PROTEIN INVOLVED IN ACTIVE TRANSPORT AND CHEMOTAXIS'''<br />
 
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==Overview==
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==CRYSTALLOGRAPHIC EVIDENCE OF A LARGE LIGAND-INDUCED HINGE-TWIST MOTION BETWEEN THE TWO DOMAINS OF THE MALTODEXTRIN-BINDING PROTEIN INVOLVED IN ACTIVE TRANSPORT AND CHEMOTAXIS==
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The periplasmic maltodextrin binding protein of Escherichia coli serves as, an initial receptor for the active transport of and chemotaxis toward, maltooligosaccharides. The three-dimensional structure of the binding, protein complexed with maltose has been previously reported [Spurlino, J., C., Lu, G.-Y., &amp; Quiocho, F. A. (1991) J. Biol. Chem. 266, 5202-5219]., Here we report the structure of the unliganded form of the binding protein, refined to 1.8-A resolution. This structure, combined with that for the, liganded form, provides the first crystallographic evidence that a major, ligand-induced conformational change occurs in a periplasmic binding, protein. The unliganded structure shows a rigid-body "hinge-bending", between the two globular domains by approximately 35 degrees, relative to, the maltose-bound structure, opening the sugar binding site groove located, between the two domains. In addition, there is an 8 degrees twist of one, domain relative to the other domain. The conformational changes observed, between this structure and the maltose-bound structure are consistent with, current models of maltose/maltodextrin transport and maltose chemotaxis, and solidify a mechanism for receptor differentiation between the, ligand-free and ligand-bound forms in signal transduction.
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<StructureSection load='1omp' size='340' side='right'caption='[[1omp]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1omp]] 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=1OMP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OMP 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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1omp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1omp OCA], [https://pdbe.org/1omp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1omp RCSB], [https://www.ebi.ac.uk/pdbsum/1omp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1omp 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/om/1omp_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=1omp 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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1OMP 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=1OMP 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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Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis., Sharff AJ, Rodseth LE, Spurlino JC, Quiocho FA, Biochemistry. 1992 Nov 10;31(44):10657-63. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1420181 1420181]
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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: periplasmic binding protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:00:42 2007''
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Current revision

CRYSTALLOGRAPHIC EVIDENCE OF A LARGE LIGAND-INDUCED HINGE-TWIST MOTION BETWEEN THE TWO DOMAINS OF THE MALTODEXTRIN-BINDING PROTEIN INVOLVED IN ACTIVE TRANSPORT AND CHEMOTAXIS

PDB ID 1omp

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