1mpr: Difference between revisions
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==MALTOPORIN FROM SALMONELLA TYPHIMURIUM== | ==MALTOPORIN FROM SALMONELLA TYPHIMURIUM== | ||
<StructureSection load='1mpr' size='340' side='right' caption='[[1mpr]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='1mpr' size='340' side='right' caption='[[1mpr]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1mpr]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1mpr]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MPR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MPR FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=1mpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mpr OCA], [http://pdbe.org/1mpr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mpr RCSB], [http://www.ebi.ac.uk/pdbsum/1mpr PDBsum]</span></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=1mpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mpr OCA], [http://pdbe.org/1mpr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mpr RCSB], [http://www.ebi.ac.uk/pdbsum/1mpr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mpr ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mp/1mpr_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mp/1mpr_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> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1mpr" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1mpr" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Salmonella | [[Category: Salmonella typhimurium]] | ||
[[Category: Meyer, J E.W]] | [[Category: Meyer, J E.W]] | ||
[[Category: Schulz, G E]] | [[Category: Schulz, G E]] | ||
Revision as of 11:06, 31 January 2018
MALTOPORIN FROM SALMONELLA TYPHIMURIUMMALTOPORIN FROM SALMONELLA TYPHIMURIUM
Structural highlights
Function[LAMB_SALTY] Involved in the transport of maltose and maltodextrins. Does not act as a receptor for phages. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe maltodextrin-specific (malto-)porin from Salmonella typhimurium has been crystallized. Its three-dimensional structure was determined at 2.4 A resolution (1 A = 0.1 nm). A comparison with the structure of the homologous porin from Escherichia coli as well as with the sequences of other related porins showed that there are regions of appreciable sequence and structure variability, despite close overall similarity. The maltoporin structure was analyzed with a bound nitrophenyl-maltotrioside as well as without ligand. Maltotrioside binding had a negligible effect on the polypeptide structure. It binds at the pore eyelet assuming a conformation close to the natural amylose helix. Structure of maltoporin from Salmonella typhimurium ligated with a nitrophenyl-maltotrioside.,Meyer JE, Hofnung M, Schulz GE J Mol Biol. 1997 Mar 7;266(4):761-75. PMID:9102468[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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