3m2l: Difference between revisions

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<StructureSection load='3m2l' size='340' side='right'caption='[[3m2l]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='3m2l' size='340' side='right'caption='[[3m2l]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3m2l]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M2L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M2L FirstGlance]. <br>
<table><tr><td colspan='2'>[[3m2l]] 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=3M2L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M2L FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hly, hla ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 "Micrococcus aureus" (Rosenbach 1884) Zopf 1885])</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]] 2.1&#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=3m2l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m2l OCA], [https://pdbe.org/3m2l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m2l RCSB], [https://www.ebi.ac.uk/pdbsum/3m2l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m2l ProSAT]</span></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=3m2l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m2l OCA], [https://pdbe.org/3m2l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m2l RCSB], [https://www.ebi.ac.uk/pdbsum/3m2l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m2l ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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.  
[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=3m2l 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=3m2l ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Engineered protein pores have several potential applications in biotechnology: as sensor elements in stochastic detection and ultrarapid DNA sequencing, as nanoreactors to observe single-molecule chemistry, and in the construction of nano- and micro-devices. One important class of pores contains molecular adapters, which provide internal binding sites for small molecules. Mutants of the alpha-hemolysin (alphaHL) pore that bind the adapter beta-cyclodextrin (betaCD) approximately 10(4) times more tightly than the wild type have been obtained. We now use single-channel electrical recording, protein engineering including unnatural amino acid mutagenesis, and high-resolution x-ray crystallography to provide definitive structural information on these engineered protein nanopores in unparalleled detail.
Molecular bases of cyclodextrin adapter interactions with engineered protein nanopores.,Banerjee A, Mikhailova E, Cheley S, Gu LQ, Montoya M, Nagaoka Y, Gouaux E, Bayley H Proc Natl Acad Sci U S A. 2010 Apr 16. PMID:20400691<ref>PMID:20400691</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3m2l" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Hemolysin 3D structures|Hemolysin 3D structures]]
*[[Hemolysin 3D structures|Hemolysin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Gouaux, E]]
[[Category: Staphylococcus aureus]]
[[Category: Montoya, M]]
[[Category: Gouaux E]]
[[Category: Beta barrel]]
[[Category: Montoya M]]
[[Category: Cytolysis]]
[[Category: Hemolysis]]
[[Category: Pore-forming toxin]]
[[Category: Secreted]]
[[Category: Toxin]]

Latest revision as of 10:23, 21 February 2024

Crystal structure of the M113F mutant of alpha-hemolysin

3m2l, resolution 2.10Å

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