2n67: Difference between revisions
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==C-terminal domain of Hemolysin II-P87M-BMRB== | |||
<StructureSection load='2n67' size='340' side='right'caption='[[2n67]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2n67]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N67 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N67 FirstGlance]. <br> | |||
</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=2n67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n67 OCA], [https://pdbe.org/2n67 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n67 RCSB], [https://www.ebi.ac.uk/pdbsum/2n67 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n67 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q81AN8_BACCR Q81AN8_BACCR] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In addition to multiple virulence factors, Bacillus cereus a pathogen that causes food poisoning and life-threatening wound infections, secretes the pore-forming toxin hemolysin II (HlyII). The HlyII toxin has a unique 94 amino acid C-terminal domain (HlyIIC). HlyIIC exhibits splitting of NMR resonances due to cis/trans isomerization of a single proline near the C-terminus. To overcome heterogeneity, we solved the structure of P405M-HlyIIC, a mutant that exclusively stabilizes the trans state. The NMR structure of HlyIIC reveals a novel fold, consisting of two subdomains alphaA-beta1-beta2 and beta3-beta4-alphaB-beta5, that come together in a barrel-like structure. The barrel core is fastened by three layers of hydrophobic residues. The barrel end opposite the HlyIIC-core has a positively charged surface, that by binding negatively charged moieties on cellular membranes, may play a role in target-cell surface recognition or stabilization of the heptameric pore complex. In the WT domain, dynamic flexibility occurs at the N-terminus and the first alpha-helix that connects the HlyIIC domain to the HlyII-core structure. In the destabilizing P405M mutant, increased flexibility is evident throughout the first subdomain, suggesting that the HlyIIC structure may have arisen through gene fusion. | |||
NMR structure of the Bacillus cereus hemolysin II C-terminal domain reveals a novel fold.,Kaplan AR, Kaus K, De S, Olson R, Alexandrescu AT Sci Rep. 2017 Jun 12;7(1):3277. doi: 10.1038/s41598-017-02917-4. PMID:28607368<ref>PMID:28607368</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 2n67" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
[[Category: | *[[Hemolysin 3D structures|Hemolysin 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacillus cereus]] | |||
[[Category: Large Structures]] | |||
[[Category: Alexandrescu AT]] | |||
[[Category: Kaplan AR]] | |||
[[Category: Maciejewski MW]] | |||
[[Category: Olson R]] | |||
Latest revision as of 09:56, 14 June 2023
C-terminal domain of Hemolysin II-P87M-BMRB
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