4yxc: Difference between revisions
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==Complex of FliM(SPOA)::FliN fusion protein and FliH(APAR)::T4lysozyme fusion protein== | ==Complex of FliM(SPOA)::FliN fusion protein and FliH(APAR)::T4lysozyme fusion protein== | ||
<StructureSection load='4yxc' size='340' side='right' caption='[[4yxc]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='4yxc' size='340' side='right'caption='[[4yxc]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4yxc]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4yxc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4], [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Enteritidis_str._SE30663 Salmonella enterica subsp. enterica serovar Enteritidis str. SE30663] and [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium_str._LT2 Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YXC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YXC 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=4yxc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yxc OCA], [https://pdbe.org/4yxc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yxc RCSB], [https://www.ebi.ac.uk/pdbsum/4yxc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yxc ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/ENLYS_BPT4 ENLYS_BPT4] Endolysin with lysozyme activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and break down the peptidoglycan layer.<ref>PMID:22389108</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 23: | Line 21: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia virus T4]] | ||
[[Category: Salmonella enterica subsp. enterica serovar | [[Category: Large Structures]] | ||
[[Category: | [[Category: Salmonella enterica subsp. enterica serovar Enteritidis str. SE30663]] | ||
[[Category: Notti | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]] | ||
[[Category: Stebbins | [[Category: Notti RQ]] | ||
[[Category: Stebbins CE]] | |||
Revision as of 10:29, 10 May 2023
Complex of FliM(SPOA)::FliN fusion protein and FliH(APAR)::T4lysozyme fusion proteinComplex of FliM(SPOA)::FliN fusion protein and FliH(APAR)::T4lysozyme fusion protein
Structural highlights
FunctionENLYS_BPT4 Endolysin with lysozyme activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and break down the peptidoglycan layer.[1] Publication Abstract from PubMedTranslocating proteins across the double membrane of Gram-negative bacteria, type III secretion systems (T3SS) occur in two evolutionarily related forms: injectisomes, delivering virulence factors into host cells, and the flagellar system, secreting the polymeric filament used for motility. While both systems share related elements of a cytoplasmic sorting platform that facilitates the hierarchical secretion of protein substrates, its assembly and regulation remain unclear. Here we describe a module mediating the assembly of the sorting platform in both secretion systems, and elucidate the structural basis for segregation of homologous components among these divergent T3SS subtypes sharing a common cytoplasmic milieu. These results provide a foundation for the subtype-specific assembly of T3SS sorting platforms and will support further mechanistic analysis and anti-virulence drug design. A common assembly module in injectisome and flagellar type III secretion sorting platforms.,Notti RQ, Bhattacharya S, Lilic M, Stebbins CE Nat Commun. 2015 May 21;6:7125. doi: 10.1038/ncomms8125. PMID:25994170[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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