1omp: Difference between revisions

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[[Image:1omp.jpg|left|200px]]<br /><applet load="1omp" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1omp, resolution 1.8&Aring;" />
'''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 />


==Overview==
==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==
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.
<StructureSection load='1omp' size='340' side='right'caption='[[1omp]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
</table>
== Function ==
[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.
== 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/om/1omp_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=1omp ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
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://oca.weizmann.ac.il/oca-bin/ocashort?id=1OMP OCA].
*[[Maltose-binding protein 3D structures|Maltose-binding protein 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Quiocho, F A.]]
[[Category: Quiocho FA]]
[[Category: Sharff, A J.]]
[[Category: Sharff AJ]]
[[Category: periplasmic binding protein]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:19:21 2008''

Latest revision as of 08:01, 14 February 2024

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

1omp, resolution 1.80Å

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