7s53

From Proteopedia

(Difference between revisions)

Current revision

Structure of Sortase A from Streptococcus pyogenes with the b7-b8 loop sequence from Listeria monocytogenes Sortase A

Structural highlights

7s53 is a 1 chain structure with sequence from Listeria monocytogenes EGD-e and Streptococcus pyogenes. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.6Å
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] Q99ZN4_STRP1

Publication Abstract from PubMed

Sequence variation in related proteins is an important characteristic that modulates activity and selectivity. An example of a protein family with a large degree of sequence variation is that of bacterial sortases, which are cysteine transpeptidases on the surface of gram-positive bacteria. Class A sortases are responsible for attachment of diverse proteins to the cell wall to facilitate environmental adaption and interaction. These enzymes are also used in protein engineering applications for sortase-mediated ligations (SML) or sortagging of protein targets. We previously investigated SrtA from Streptococcus pneumoniae, identifying a number of putative beta7-beta8 loop-mediated interactions that affected in vitro enzyme function. We identified residues that contributed to the ability of S. pneumoniae SrtA to recognize several amino acids at the P1' position of the substrate motif, underlined in LPXTG, in contrast to the strict P1' Gly recognition of SrtA from Staphylococcus aureus. However, motivated by the lack of a structural model for the active, monomeric form of S. pneumoniae SrtA, here, we expanded our studies to other Streptococcus SrtA proteins. We solved the first monomeric structure of S. agalactiae SrtA which includes the C-terminus, and three others of beta7-beta8 loop chimeras from S. pyogenes and S. agalactiae SrtA. These structures and accompanying biochemical data support our previously identified beta7-beta8 loop-mediated interactions and provide additional insight into their role in Class A sortase substrate selectivity. A greater understanding of individual SrtA sequence and structural determinants of target selectivity may also facilitate the design or discovery of improved sortagging tools.

Structural and biochemical analyses of selectivity determinants in chimeric Streptococcus Class A sortase enzymes.,Gao M, Johnson DA, Piper IM, Kodama HM, Svendsen JE, Tahti E, Longshore-Neate F, Vogel B, Antos JM, Amacher JF Protein Sci. 2021 Dec 22. doi: 10.1002/pro.4266. PMID:34939250^[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
↑ Gao M, Johnson DA, Piper IM, Kodama HM, Svendsen JE, Tahti E, Longshore-Neate F, Vogel B, Antos JM, Amacher JF. Structural and biochemical analyses of selectivity determinants in chimeric Streptococcus Class A sortase enzymes. Protein Sci. 2021 Dec 22. doi: 10.1002/pro.4266. PMID:34939250 doi:http://dx.doi.org/10.1002/pro.4266

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/7s53"

@@ Line 3: / Line 3: @@
 <StructureSection load='7s53' size='340' side='right'caption='[[7s53]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[7s53]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7S53 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7S53 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[7s53]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Listeria_monocytogenes_EGD-e Listeria monocytogenes EGD-e] and [https://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7S53 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7S53 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=7s53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7s53 OCA], [https://pdbe.org/7s53 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7s53 RCSB], [https://www.ebi.ac.uk/pdbsum/7s53 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7s53 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]] 1.6&#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=7s53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7s53 OCA], [https://pdbe.org/7s53 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7s53 RCSB], [https://www.ebi.ac.uk/pdbsum/7s53 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7s53 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> [https://www.uniprot.org/uniprot/Q99ZN4_STRP1 Q99ZN4_STRP1]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 20: / Line 23: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Amacher, J F]]
+[[Category: Listeria monocytogenes EGD-e]]
-[[Category: Antos, J M]]
+[[Category: Streptococcus pyogenes]]
-[[Category: Johnson, D A]]
+[[Category: Amacher JF]]
-[[Category: Svendsen, J E]]
+[[Category: Antos JM]]
-[[Category: Eight-stranded beta barrel]]
+[[Category: Johnson DA]]
-[[Category: Housekeeping sortase]]
+[[Category: Svendsen JE]]
-[[Category: Hydrolase]]
-[[Category: Sortase]]
-[[Category: Sortase-fold]]
-[[Category: Surface protein]]
-[[Category: Transpeptidase]]

7s53

From Proteopedia

Current revision

Structure of Sortase A from Streptococcus pyogenes with the b7-b8 loop sequence from 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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