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[[Image:1mdp.gif|left|200px]]


{{Structure
==REFINED STRUCTURES OF TWO INSERTION(SLASH)DELETION MUTANTS PROBE FUNCTION OF THE MALTODEXTRIN BINDING PROTEIN==
|PDB= 1mdp |SIZE=350|CAPTION= <scene name='initialview01'>1mdp</scene>, resolution 2.3&Aring;
<StructureSection load='1mdp' size='340' side='right'caption='[[1mdp]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=MAL:MALTOSE'>MAL</scene>
<table><tr><td colspan='2'>[[1mdp]] is a 2 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=1MDP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MDP FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
|GENE=  
<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_900001:alpha-maltose'>PRD_900001</scene></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=1mdp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mdp OCA], [https://pdbe.org/1mdp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mdp RCSB], [https://www.ebi.ac.uk/pdbsum/1mdp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mdp 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/md/1mdp_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=1mdp ConSurf].
<div style="clear:both"></div>


'''REFINED STRUCTURES OF TWO INSERTION(SLASH)DELETION MUTANTS PROBE FUNCTION OF THE MALTODEXTRIN BINDING PROTEIN'''
==See Also==
 
*[[Maltose-binding protein 3D structures|Maltose-binding protein 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
The X-ray structures of the maltose bound forms of two insertion/deletion mutants of the Escherichia coli maltodextrin binding protein, MalE322 and MalE178, have been determined and refined. MalE322 involves a one residue deletion, two residue insertion in a hinge segment connecting the two (N and C) domains of the protein, an area already identified as being critical for the correct functioning of the protein. MalE178 involves a nine residue deletion and two residue insertion in a helix at the periphery of the C-domain. The function of both mutant proteins is similar to the wild-type, although MalE322 increases the ability to transport maltose and maltodextrin whilst inhibiting the ability of the cell to grow on dextrins. Both proteins exhibit very localized and conservative conformational changes due to their mutations. The structure of MalE322 shows some deformation of the third hinge strand, indicating the likely cause of change in its biochemistry. MalE178 is stable and its activity virtually unchanged from the wild-type. This is most likely due to the long distance of the mutation from the binding site and conservation of the number of interactions between the area around the deletion site and the main body of the protein.
 
==About this Structure==
1MDP is a [[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=1MDP OCA].
 
==Reference==
Refined structures of two insertion/deletion mutants probe function of the maltodextrin binding protein., Sharff AJ, Rodseth LE, Szmelcman S, Hofnung M, Quiocho FA, J Mol Biol. 1995 Feb 10;246(1):8-13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7853407 7853407]
[[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: MAL]]
[[Category: sugar transport]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:42:13 2008''

Latest revision as of 10:43, 14 February 2024

REFINED STRUCTURES OF TWO INSERTION(SLASH)DELETION MUTANTS PROBE FUNCTION OF THE MALTODEXTRIN BINDING PROTEINREFINED STRUCTURES OF TWO INSERTION(SLASH)DELETION MUTANTS PROBE FUNCTION OF THE MALTODEXTRIN BINDING PROTEIN

Structural highlights

1mdp is a 2 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 2.3Å
Ligands:,
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

1mdp, resolution 2.30Å

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