1mpc

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(New page: 200px<br /><applet load="1mpc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mpc, resolution 2.1&Aring;" /> '''MALTODEXTRIN-BINDING ...)
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[[Image:1mpc.jpg|left|200px]]<br /><applet load="1mpc" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1mpc, resolution 2.1&Aring;" />
 
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'''MALTODEXTRIN-BINDING PROTEIN (MALTOSE-BINDING PROTEIN) MUTANT, WITH ARGININE REPLACING TRYPTOPHAN AT POSITION 230 (TRP-230-ARG)'''<br />
 
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==Overview==
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==MALTODEXTRIN-BINDING PROTEIN (MALTOSE-BINDING PROTEIN) MUTANT, WITH ARGININE REPLACING TRYPTOPHAN AT POSITION 230 (TRP-230-ARG)==
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A mutant of the periplasmic maltose-binding protein (MBP) with altered, transport properties was studied. A change of residue 230 from tryptophan, to arginine results in dominant-negative MBP: expression of this protein, against a wild-type background causes inhibition of maltose transport. As, part of an investigation of the mechanism of such inhibition, we have, solved crystal structures of both unliganded and liganded mutant protein., In the closed, liganded conformation, the side-chain of R230 projects into, a region of the surface of MBP that has been identified as important for, transport while in the open form, the same side-chain takes on a, different, and less ordered, conformation. The crystallographic work is, supplemented with a small-angle X-ray scattering study that provides, evidence that the solution conformation of unliganded mutant is similar to, that of wild-type MBP. It is concluded that dominant-negative inhibition, of maltose transport must result from the formation of a non-productive, complex between liganded-bound mutant MBP and wild-type MalFGK2. A general, kinetic framework for transport by either wild-type MalFGK2 or, MBP-independent MalFGK2 is used to understand the effects of, dominant-negative MBP molecules on both of these systems.
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<StructureSection load='1mpc' size='340' side='right'caption='[[1mpc]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1mpc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MPC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MPC 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]] 2.1&#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=1mpc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mpc OCA], [https://pdbe.org/1mpc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mpc RCSB], [https://www.ebi.ac.uk/pdbsum/1mpc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mpc 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/mp/1mpc_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=1mpc 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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1MPC 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=1MPC 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 and solution conformations of a dominant-negative mutant of Escherichia coli maltose-binding protein., Shilton BH, Shuman HA, Mowbray SL, J Mol Biol. 1996 Nov 29;264(2):364-76. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8951382 8951382]
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[[Category: Escherichia coli K-12]]
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[[Category: Escherichia coli]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Mowbray SL]]
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[[Category: Mowbray, S.L.]]
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[[Category: Shilton BH]]
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[[Category: Shilton, B.H.]]
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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 21:36:15 2007''
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Current revision

MALTODEXTRIN-BINDING PROTEIN (MALTOSE-BINDING PROTEIN) MUTANT, WITH ARGININE REPLACING TRYPTOPHAN AT POSITION 230 (TRP-230-ARG)

PDB ID 1mpc

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