1omp: Difference between revisions

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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==
==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==
<StructureSection load='1omp' size='340' side='right' caption='[[1omp]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='1omp' size='340' side='right'caption='[[1omp]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1omp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OMP FirstGlance]. <br>
<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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1omp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1omp OCA], [http://pdbe.org/1omp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1omp RCSB], [http://www.ebi.ac.uk/pdbsum/1omp PDBsum]</span></td></tr>
</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>
</table>
== Function ==
== Function ==
[[http://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.  
[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/om/1omp_consurf.spt"</scriptWhenChecked>
     <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>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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/chain_selection.php?pdb_ID=2ata ConSurf].
</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>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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:1420181<ref>PMID:1420181</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1omp" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Maltose-binding protein|Maltose-binding protein]]
*[[Maltose-binding protein 3D structures|Maltose-binding protein 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus coli migula 1895]]
[[Category: Escherichia coli]]
[[Category: Quiocho, F A]]
[[Category: Large Structures]]
[[Category: Sharff, A J]]
[[Category: Quiocho FA]]
[[Category: Periplasmic binding protein]]
[[Category: Sharff AJ]]

Latest revision as of 11:01, 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 CHEMOTAXISCRYSTALLOGRAPHIC EVIDENCE OF A LARGE LIGAND-INDUCED HINGE-TWIST MOTION BETWEEN THE TWO DOMAINS OF THE MALTODEXTRIN-BINDING PROTEIN INVOLVED IN ACTIVE TRANSPORT AND CHEMOTAXIS

Structural highlights

1omp is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1omp, resolution 1.80Å

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