3m4e: Difference between revisions
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New page: '''Unreleased structure''' The entry 3m4e is ON HOLD Authors: Montoya, M., Gouaux, E. Description: Crystal structure of the M113N mutant of alpha-hemolysin bound to beta-cyclodextrin ... |
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==Crystal structure of the M113N mutant of alpha-hemolysin bound to beta-cyclodextrin== | |||
<StructureSection load='3m4e' size='340' side='right'caption='[[3m4e]], [[Resolution|resolution]] 2.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3m4e]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M4E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M4E 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]] 2.3Å</td></tr> | |||
<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_900012:beta-cyclodextrin'>PRD_900012</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=3m4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m4e OCA], [https://pdbe.org/3m4e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m4e RCSB], [https://www.ebi.ac.uk/pdbsum/3m4e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m4e ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/HLA_STAAU HLA_STAAU] Alpha-toxin binds to the membrane of eukaryotic cells resulting in the release of low-molecular weight molecules and leading to an eventual osmotic lysis. Heptamer oligomerization and pore formation is required for lytic activity. | |||
== 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/m4/3m4e_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=3m4e ConSurf]. | |||
<div style="clear:both"></div> | |||
==See Also== | |||
*[[Hemolysin 3D structures|Hemolysin 3D structures]] | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Staphylococcus aureus]] | |||
[[Category: Gouaux E]] | |||
[[Category: Montoya M]] | |||
Latest revision as of 13:23, 21 February 2024
Crystal structure of the M113N mutant of alpha-hemolysin bound to beta-cyclodextrinCrystal structure of the M113N mutant of alpha-hemolysin bound to beta-cyclodextrin
Structural highlights
FunctionHLA_STAAU Alpha-toxin binds to the membrane of eukaryotic cells resulting in the release of low-molecular weight molecules and leading to an eventual osmotic lysis. Heptamer oligomerization and pore formation is required for lytic activity. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also |
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