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5hu4

From Proteopedia

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Current revision

Cystal structure of listeria monocytogenes sortase A

Structural highlights

5hu4 is a 1 chain structure with sequence from Listeria monocytogenes. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.3Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SRTA_LISMO Transpeptidase that anchors surface proteins to the cell wall (PubMed:11854224, PubMed:11929538, PubMed:16247833, PubMed:22837151). Recognizes and modifies its substrate by proteolytic cleavage of a C-terminal sorting signal. Following cleavage, a covalent intermediate is formed via a thioester bond between the sortase and its substrate, which is then transferred and covalently attached to the cell wall (Probable). This sortase recognizes a Leu-Pro-x-Thr-Gly (LPXTG) motif, which is cleaved by the sortase between the threonine and glycine residues (PubMed:11929538). Involved in pathogenesis (PubMed:11854224, PubMed:11929538, PubMed:15028680). May regulate the rate of synthesis and/or the stability of a subset of LPXTG proteins (PubMed:22837151). Not involved in cell wall-anchoring of Hbp2 (SvpA) or Hbp1 (PubMed:15028680, PubMed:16247833).^[1] ^[2] ^[3] ^[4] ^[5] ^[6]

Publication Abstract from PubMed

The critical role of sortase A in gram-positive bacterial pathogenicity makes this protein a good potential target for antimicrobial therapy. In this study, we report for the first time the crystal structure of Listeria monocytogenes sortase A and identify the active sites that mediate its transpeptidase activity. We also used a sortase A (SrtA) enzyme activity inhibition assay, simulation, and isothermal titration calorimetry analysis to discover that chalcone, an agent with little anti-L. monocytogenes activity, could significantly inhibit sortase A activity with an IC50 of 28.41 +/- 5.34 muM by occupying the active site of SrtA. The addition of chalcone to a co-culture of L. monocytogenes and Caco-2 cells significantly inhibited bacterial entry into the cells and L. monocytogenes-mediated cytotoxicity. Additionally, chalcone treatment decreased the mortality of infected mice, the bacterial burden in target organs, and the pathological damage to L. monocytogenes-infected mice. In conclusion, these findings suggest that chalcone is a promising candidate for the development of treatment against L. monocytogenes infection.

Inhibition of sortase A by chalcone prevents Listeria monocytogenes infection.,Li H, Chen Y, Zhang B, Niu X, Song M, Luo Z, Lu G, Liu B, Zhao X, Wang J, Deng X Biochem Pharmacol. 2016 Apr 15;106:19-29. doi: 10.1016/j.bcp.2016.01.018. Epub, 2016 Jan 28. PMID:26826492^[7]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Garandeau C, Réglier-Poupet H, Dubail I, Beretti JL, Berche P, Charbit A. The sortase SrtA of Listeria monocytogenes is involved in processing of internalin and in virulence. Infect Immun. 2002 Mar;70(3):1382-90. PMID:11854224 doi:10.1128/IAI.70.3.1382-1390.2002
↑ Bierne H, Mazmanian SK, Trost M, Pucciarelli MG, Liu G, Dehoux P, Jänsch L, Garcia-del Portillo F, Schneewind O, Cossart P. Inactivation of the srtA gene in Listeria monocytogenes inhibits anchoring of surface proteins and affects virulence. Mol Microbiol. 2002 Feb;43(4):869-81. PMID:11929538 doi:10.1046/j.1365-2958.2002.02798.x
↑ Bierne H, Garandeau C, Pucciarelli MG, Sabet C, Newton S, Garcia-del Portillo F, Cossart P, Charbit A. Sortase B, a new class of sortase in Listeria monocytogenes. J Bacteriol. 2004 Apr;186(7):1972-82. PMID:15028680 doi:10.1128/JB.186.7.1972-1982.2004
↑ Pucciarelli MG, Calvo E, Sabet C, Bierne H, Cossart P, García-del Portillo F. Identification of substrates of the Listeria monocytogenes sortases A and B by a non-gel proteomic analysis. Proteomics. 2005 Dec;5(18):4808-17. PMID:16247833 doi:10.1002/pmic.200402075
↑ Mariscotti JF, Quereda JJ, Pucciarelli MG. Contribution of sortase A to the regulation of Listeria monocytogenes LPXTG surface proteins. Int Microbiol. 2012 Mar;15(1):43-51. PMID:22837151 doi:10.2436/20.1501.01.157
↑ Bierne H, Mazmanian SK, Trost M, Pucciarelli MG, Liu G, Dehoux P, Jänsch L, Garcia-del Portillo F, Schneewind O, Cossart P. Inactivation of the srtA gene in Listeria monocytogenes inhibits anchoring of surface proteins and affects virulence. Mol Microbiol. 2002 Feb;43(4):869-81. PMID:11929538 doi:10.1046/j.1365-2958.2002.02798.x
↑ Li H, Chen Y, Zhang B, Niu X, Song M, Luo Z, Lu G, Liu B, Zhao X, Wang J, Deng X. Inhibition of sortase A by chalcone prevents Listeria monocytogenes infection. Biochem Pharmacol. 2016 Apr 15;106:19-29. doi: 10.1016/j.bcp.2016.01.018. Epub, 2016 Jan 28. PMID:26826492 doi:http://dx.doi.org/10.1016/j.bcp.2016.01.018

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5hu4"

Categories: Large Structures | Listeria monocytogenes | Li H

@@ Line 1: / Line 1: @@
 ==Cystal structure of listeria monocytogenes sortase A==
-<StructureSection load='5hu4' size='340' side='right' caption='[[5hu4]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+<StructureSection load='5hu4' size='340' side='right'caption='[[5hu4]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5hu4]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HU4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HU4 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5hu4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HU4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HU4 FirstGlance]. <br>
-</td></tr><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=5hu4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hu4 OCA], [http://pdbe.org/5hu4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hu4 RCSB], [http://www.ebi.ac.uk/pdbsum/5hu4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hu4 ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#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=5hu4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hu4 OCA], [https://pdbe.org/5hu4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hu4 RCSB], [https://www.ebi.ac.uk/pdbsum/5hu4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hu4 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/SRTA_LISMO SRTA_LISMO] Transpeptidase that anchors surface proteins to the cell wall (PubMed:11854224, PubMed:11929538, PubMed:16247833, PubMed:22837151). Recognizes and modifies its substrate by proteolytic cleavage of a C-terminal sorting signal. Following cleavage, a covalent intermediate is formed via a thioester bond between the sortase and its substrate, which is then transferred and covalently attached to the cell wall (Probable). This sortase recognizes a Leu-Pro-x-Thr-Gly (LPXTG) motif, which is cleaved by the sortase between the threonine and glycine residues (PubMed:11929538). Involved in pathogenesis (PubMed:11854224, PubMed:11929538, PubMed:15028680). May regulate the rate of synthesis and/or the stability of a subset of LPXTG proteins (PubMed:22837151). Not involved in cell wall-anchoring of Hbp2 (SvpA) or Hbp1 (PubMed:15028680, PubMed:16247833).<ref>PMID:11854224</ref> <ref>PMID:11929538</ref> <ref>PMID:15028680</ref> <ref>PMID:16247833</ref> <ref>PMID:22837151</ref> <ref>PMID:11929538</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 19: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Li, H]]
+[[Category: Large Structures]]
-[[Category: Hydrolase]]
+[[Category: Listeria monocytogenes]]
-[[Category: Protease]]
+[[Category: Li H]]
-[[Category: Sortase some]]

5hu4

From Proteopedia

Current revision

Cystal structure of listeria monocytogenes sortase A

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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