View source for 7nmq


==Bacillus cereus HblL1 toxin component==
<StructureSection load='7nmq' size='340' side='right'caption='[[7nmq]], [[Resolution|resolution]] 1.36&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7nmq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7NMQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NMQ 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]] 1.36&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=7nmq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7nmq OCA], [https://pdbe.org/7nmq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7nmq RCSB], [https://www.ebi.ac.uk/pdbsum/7nmq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7nmq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q1XBV1_BACCE Q1XBV1_BACCE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Hbl toxin is a three-component haemolytic complex produced by Bacillus cereus sensu lato strains and implicated as a cause of diarrhoea in B. cereus food poisoning. While the structure of the HblB component of this toxin is known, the structures of the other components are unresolved. Here, we describe the expression of the recombinant HblL1 component and the elucidation of its structure to 1.36 A. Like HblB, it is a member of the alpha-helical pore-forming toxin family. In comparison to other members of this group, it has an extended hydrophobic beta tongue region that may be involved in pore formation. Molecular docking was used to predict possible interactions between HblL1 and HblB, and suggests a head to tail dimer might form, burying the HblL1 beta tongue region.

The Crystal Structure of Bacillus cereus HblL1.,Worthy HL, Williamson LJ, Auhim HS, Leppla SH, Sastalla I, Jones DD, Rizkallah PJ, Berry C Toxins (Basel). 2021 Mar 31;13(4). pii: toxins13040253. doi:, 10.3390/toxins13040253. PMID:33807365<ref>PMID:33807365</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7nmq" style="background-color:#fffaf0;"></div>

==See Also==
*[[Hemolysin 3D structures|Hemolysin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus cereus]]
[[Category: Large Structures]]
[[Category: Berry C]]
[[Category: Rizkallah PJ]]