6wa1: Difference between revisions
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==Dimeric form of the trans-stabilized Hemolysin II C-terminal domain== | ==Dimeric form of the trans-stabilized Hemolysin II C-terminal domain== | ||
<StructureSection load='6wa1' size='340' side='right'caption='[[6wa1 | <StructureSection load='6wa1' size='340' side='right'caption='[[6wa1]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6wa1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[6wa1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus_ATCC_14579 Bacillus cereus ATCC 14579]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6WA1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6WA1 FirstGlance]. <br> | ||
</td></tr> | </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=6wa1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wa1 OCA], [https://pdbe.org/6wa1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6wa1 RCSB], [https://www.ebi.ac.uk/pdbsum/6wa1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6wa1 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=6wa1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wa1 OCA], [https://pdbe.org/6wa1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6wa1 RCSB], [https://www.ebi.ac.uk/pdbsum/6wa1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6wa1 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q81AN8_BACCR Q81AN8_BACCR] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 6wa1" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6wa1" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Hemolysin 3D structures|Hemolysin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bacillus cereus ATCC 14579]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Alexandrescu | [[Category: Alexandrescu AT]] | ||
[[Category: Kaplan | [[Category: Kaplan AR]] | ||
Latest revision as of 14:06, 14 June 2023
Dimeric form of the trans-stabilized Hemolysin II C-terminal domainDimeric form of the trans-stabilized Hemolysin II C-terminal domain
Structural highlights
FunctionPublication Abstract from PubMedThe C-terminal domain of Bacillus cereus hemolysin II (HlyIIC), stabilizes the trans-membrane-pore formed by the HlyII toxin and may aid in target cell recognition. Initial efforts to determine the NMR structure of HlyIIC were hampered by cis/trans isomerization about the single proline at position 405 that leads to doubling of NMR resonances. We used the mutant P405M-HlyIIC that eliminates the cis proline to determine the NMR structure of the domain, which revealed a novel fold. Here, we extend earlier studies to the NMR structure determination of the cis and trans states of WT-HlyIIC that exist simultaneously in solution. The primary structural differences between the cis and trans states are in the loop that contains P405, and structurally adjacent loops. Thermodynamic linkage analysis shows that at 25 C the cis proline, which already has a large fraction of 20% in the unfolded protein, increases to 50% in the folded state due to coupling with the global stability of the domain. The P405M or P405A substitutions eliminate heterogeneity due to proline isomerization but lead to the formation of a new dimeric species. The NMR structure of the dimer shows that it is formed through domain-swapping of strand beta5, the last segment of secondary structure following P405. The presence of P405 in WT-HlyIIC strongly disfavors the dimer compared to the P405M-HlyIIC or P405A-HlyIIC mutants. The WT proline may thus act as a "gatekeeper," warding off aggregative misfolding. Protein yoga: Conformational versatility of the Hemolysin II C-terminal domain detailed by NMR structures for multiple states.,Kaplan AR, Olson R, Alexandrescu AT Protein Sci. 2021 Mar 17. doi: 10.1002/pro.4066. PMID:33733504[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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