8hhe: Difference between revisions

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'''Unreleased structure'''


The entry 8hhe is ON HOLD
==Crystal structure of Cry5B from Bacillus thuringiensis at 4.5 A resolution==
<StructureSection load='8hhe' size='340' side='right'caption='[[8hhe]], [[Resolution|resolution]] 4.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8hhe]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_thuringiensis_YBT-1518 Bacillus thuringiensis YBT-1518]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HHE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HHE 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]] 4.5&#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=8hhe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hhe OCA], [https://pdbe.org/8hhe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hhe RCSB], [https://www.ebi.ac.uk/pdbsum/8hhe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hhe ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B7SB31_BACTU B7SB31_BACTU]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal protein Cry5B, a pore-forming protein produced by the soil bacterium Bacillus thuringiensis, has been demonstrated to have excellent anthelmintic activity. While a previous structure of the three-domain core region of Cry5B(112-698) had been reported, this structure lacked a key N-terminal extension critical to function. Here we report the structure of Cry5B(27-698) containing this N-terminal extension. This new structure adopts a distinct quaternary structure compared to the previous Cry5B(112-698) structure, and also exhibits a change in the conformation of residues 112-140 involved in linking the N-terminal extension to the three-domain core by forming a random coil and an extended alpha-helix. A role for the N-terminal extension is suggested based on a computational model of the tetramer with the conformation of residues 112-140 in its alternate alpha-helix conformation. Finally, based on the Cry5B(27-698) structure, site-directed mutagenesis studies were performed on Tyr495, which revealed that having an aromatic group or bulky group at this residue 495 is important for Cry5B toxicity.


Authors: Li, J., Chan, M.K.
Insights from the Structure of an Active Form of Bacillus thuringiensis Cry5B.,Li J, Wang L, Kotaka M, Lee MM, Chan MK Toxins (Basel). 2022 Nov 23;14(12):823. doi: 10.3390/toxins14120823. PMID:36548720<ref>PMID:36548720</ref>


Description: Crystal structure of Cry5B from Bacillus thuringiensis at 4.5 A resolution
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Li, J]]
<div class="pdbe-citations 8hhe" style="background-color:#fffaf0;"></div>
[[Category: Chan, M.K]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus thuringiensis YBT-1518]]
[[Category: Large Structures]]
[[Category: Chan MK]]
[[Category: Li J]]
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