6sb5: Difference between revisions

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'''Unreleased structure'''


The entry 6sb5 is ON HOLD
==CryoEM structure of murine perforin-2 ectodomain in a pore form==
 
<StructureSection load='6sb5' size='340' side='right'caption='[[6sb5]], [[Resolution|resolution]] 5.00&Aring;' scene=''>
Authors:  
== Structural highlights ==
 
<table><tr><td colspan='2'>[[6sb5]] is a 16 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SB5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6SB5 FirstGlance]. <br>
Description:  
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
[[Category: Unreleased Structures]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6sb5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sb5 OCA], [http://pdbe.org/6sb5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6sb5 RCSB], [http://www.ebi.ac.uk/pdbsum/6sb5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6sb5 ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/MPEG1_MOUSE MPEG1_MOUSE]] Plays a key role in the innate immune response following bacterial infection by polymerizing and inserting into the bacterial surface to form pores (PubMed:26402460). By breaching the surface of phagocytosed bacteria, allows antimicrobial effectors to enter the bacterial periplasmic space and degrade bacterial proteins such as superoxide dismutase sodC which contributes to bacterial virulence (PubMed:30249808). Shows antibacterial activity against a wide spectrum of Gram-positive, Gram-negative and acid-fast bacteria (PubMed:23257510, PubMed:23753625, PubMed:26402460). Reduces the viability of the intracytosolic pathogen L.monocytogenes by inhibiting acidification of the phagocytic vacuole of host cells which restricts bacterial translocation from the vacuole to the cytosol (PubMed:26831467). Required for the antibacterial activity of reactive oxygen species and nitric oxide (PubMed:26402460).<ref>PMID:23257510</ref> <ref>PMID:23753625</ref> <ref>PMID:26402460</ref> <ref>PMID:26831467</ref> <ref>PMID:30249808</ref> 
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Gilbert, R J.C]]
[[Category: Ni, T]]
[[Category: Yu, X]]
[[Category: Macpf]]
[[Category: Pore-forming protein]]
[[Category: Pre-pore]]
[[Category: Toxin]]

Revision as of 11:09, 5 February 2020

CryoEM structure of murine perforin-2 ectodomain in a pore formCryoEM structure of murine perforin-2 ectodomain in a pore form

Structural highlights

6sb5 is a 16 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MPEG1_MOUSE] Plays a key role in the innate immune response following bacterial infection by polymerizing and inserting into the bacterial surface to form pores (PubMed:26402460). By breaching the surface of phagocytosed bacteria, allows antimicrobial effectors to enter the bacterial periplasmic space and degrade bacterial proteins such as superoxide dismutase sodC which contributes to bacterial virulence (PubMed:30249808). Shows antibacterial activity against a wide spectrum of Gram-positive, Gram-negative and acid-fast bacteria (PubMed:23257510, PubMed:23753625, PubMed:26402460). Reduces the viability of the intracytosolic pathogen L.monocytogenes by inhibiting acidification of the phagocytic vacuole of host cells which restricts bacterial translocation from the vacuole to the cytosol (PubMed:26831467). Required for the antibacterial activity of reactive oxygen species and nitric oxide (PubMed:26402460).[1] [2] [3] [4] [5]

References

  1. ↑ McCormack R, de Armas LR, Shiratsuchi M, Ramos JE, Podack ER. Inhibition of intracellular bacterial replication in fibroblasts is dependent on the perforin-like protein (perforin-2) encoded by macrophage-expressed gene 1. J Innate Immun. 2013;5(2):185-94. doi: 10.1159/000345249. Epub 2012 Dec 15. PMID:23257510 doi:http://dx.doi.org/10.1159/000345249
  2. ↑ Fields KA, McCormack R, de Armas LR, Podack ER. Perforin-2 restricts growth of Chlamydia trachomatis in macrophages. Infect Immun. 2013 Aug;81(8):3045-54. doi: 10.1128/IAI.00497-13. Epub 2013 Jun, 10. PMID:23753625 doi:http://dx.doi.org/10.1128/IAI.00497-13
  3. ↑ McCormack RM, de Armas LR, Shiratsuchi M, Fiorentino DG, Olsson ML, Lichtenheld MG, Morales A, Lyapichev K, Gonzalez LE, Strbo N, Sukumar N, Stojadinovic O, Plano GV, Munson GP, Tomic-Canic M, Kirsner RS, Russell DG, Podack ER. Perforin-2 is essential for intracellular defense of parenchymal cells and phagocytes against pathogenic bacteria. Elife. 2015 Sep 24;4. doi: 10.7554/eLife.06508. PMID:26402460 doi:http://dx.doi.org/10.7554/eLife.06508
  4. ↑ McCormack R, Bahnan W, Shrestha N, Boucher J, Barreto M, Barrera CM, Dauer EA, Freitag NE, Khan WN, Podack ER, Schesser K. Perforin-2 Protects Host Cells and Mice by Restricting the Vacuole to Cytosol Transitioning of a Bacterial Pathogen. Infect Immun. 2016 Mar 24;84(4):1083-1091. doi: 10.1128/IAI.01434-15. Print 2016 , Apr. PMID:26831467 doi:http://dx.doi.org/10.1128/IAI.01434-15
  5. ↑ Bai F, McCormack RM, Hower S, Plano GV, Lichtenheld MG, Munson GP. Perforin-2 Breaches the Envelope of Phagocytosed Bacteria Allowing Antimicrobial Effectors Access to Intracellular Targets. J Immunol. 2018 Nov 1;201(9):2710-2720. doi: 10.4049/jimmunol.1800365. Epub 2018 , Sep 24. PMID:30249808 doi:http://dx.doi.org/10.4049/jimmunol.1800365

6sb5, resolution 5.00Å

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