7s54

From Proteopedia

(Difference between revisions)

Current revision

Sortase A from Streptococcus agalactiae with the deltaN188 b7-b8 loop sequence from Staphylococcus aureus Sortase A

Structural highlights

7s54 is a 2 chain structure with sequence from Staphylococcus aureus subsp. aureus NCTC 8325 and Streptococcus agalactiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.794Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SRTA_STAA8 Transpeptidase that anchors surface proteins to the cell wall (PubMed:10427003, PubMed:10446208, PubMed:10535938, PubMed:11714722, PubMed:14769030, PubMed:15247224). 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 (PubMed:10446208, PubMed:10535938, PubMed:11714722, PubMed:14769030, PubMed:15247224). This sortase recognizes a Leu-Pro-x-Thr-Gly (LPXTG) motif, which is cleaved by the sortase between the threonine and glycine residues (PubMed:10535938, PubMed:11714722, PubMed:14769030, PubMed:15247224). Utilizes lipid II as the peptidoglycan substrate for the sorting reaction (PubMed:10446208, PubMed:11856734). Responsible for the display of important virulence factors (PubMed:14769030). Important for interactions with the host and host colonization during infection (PubMed:10805806, PubMed:14769030).^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] ^[8] SRTA_STRA3 Transpeptidase that anchors surface proteins to the cell wall. 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. This sortase recognizes a Leu-Pro-x-Thr-Gly (LPXTG) motif, which is cleaved by the sortase between the threonine and glycine residues (By similarity). Essential for adherence to eukaryotic cells and for binding to fibronectin and fibrinogen (PubMed:15908360).[UniProtKB:Q2FV99]^[9]

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^[10]

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

References

↑ Mazmanian SK, Liu G, Ton-That H, Schneewind O. Staphylococcus aureus sortase, an enzyme that anchors surface proteins to the cell wall. Science. 1999 Jul 30;285(5428):760-3. PMID:10427003
↑ Ton-That H, Schneewind O. Anchor structure of staphylococcal surface proteins. IV. Inhibitors of the cell wall sorting reaction. J Biol Chem. 1999 Aug 20;274(34):24316-20. doi: 10.1074/jbc.274.34.24316. PMID:10446208 doi:http://dx.doi.org/10.1074/jbc.274.34.24316
↑ Ton-That H, Liu G, Mazmanian SK, Faull KF, Schneewind O. Purification and characterization of sortase, the transpeptidase that cleaves surface proteins of Staphylococcus aureus at the LPXTG motif. Proc Natl Acad Sci U S A. 1999 Oct 26;96(22):12424-9. doi:, 10.1073/pnas.96.22.12424. PMID:10535938 doi:http://dx.doi.org/10.1073/pnas.96.22.12424
↑ Mazmanian SK, Liu G, Jensen ER, Lenoy E, Schneewind O. Staphylococcus aureus sortase mutants defective in the display of surface proteins and in the pathogenesis of animal infections. Proc Natl Acad Sci U S A. 2000 May 9;97(10):5510-5. doi: 10.1073/pnas.080520697. PMID:10805806 doi:http://dx.doi.org/10.1073/pnas.080520697
↑ Ton-That H, Mazmanian SK, Alksne L, Schneewind O. Anchoring of surface proteins to the cell wall of Staphylococcus aureus. Cysteine 184 and histidine 120 of sortase form a thiolate-imidazolium ion pair for catalysis. J Biol Chem. 2002 Mar 1;277(9):7447-52. doi: 10.1074/jbc.M109945200. Epub 2001, Nov 19. PMID:11714722 doi:http://dx.doi.org/10.1074/jbc.M109945200
↑ Perry AM, Ton-That H, Mazmanian SK, Schneewind O. Anchoring of surface proteins to the cell wall of Staphylococcus aureus. III. Lipid II is an in vivo peptidoglycan substrate for sortase-catalyzed surface protein anchoring. J Biol Chem. 2002 May 3;277(18):16241-8. doi: 10.1074/jbc.M109194200. Epub 2002, Feb 20. PMID:11856734 doi:http://dx.doi.org/10.1074/jbc.M109194200
↑ Kruger RG, Otvos B, Frankel BA, Bentley M, Dostal P, McCafferty DG. Analysis of the substrate specificity of the Staphylococcus aureus sortase transpeptidase SrtA. Biochemistry. 2004 Feb 17;43(6):1541-51. doi: 10.1021/bi035920j. PMID:14769030 doi:http://dx.doi.org/10.1021/bi035920j
↑ Marraffini LA, Ton-That H, Zong Y, Narayana SV, Schneewind O. Anchoring of surface proteins to the cell wall of Staphylococcus aureus. A conserved arginine residue is required for efficient catalysis of sortase A. J Biol Chem. 2004 Sep 3;279(36):37763-70. doi: 10.1074/jbc.M405282200. Epub 2004 , Jul 6. PMID:15247224 doi:http://dx.doi.org/10.1074/jbc.M405282200
↑ Lalioui L, Pellegrini E, Dramsi S, Baptista M, Bourgeois N, Doucet-Populaire F, Rusniok C, Zouine M, Glaser P, Kunst F, Poyart C, Trieu-Cuot P. The SrtA Sortase of Streptococcus agalactiae is required for cell wall anchoring of proteins containing the LPXTG motif, for adhesion to epithelial cells, and for colonization of the mouse intestine. Infect Immun. 2005 Jun;73(6):3342-50. PMID:15908360 doi:10.1128/IAI.73.6.3342-3350.2005
↑ 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/7s54"

@@ Line 3: / Line 3: @@
 <StructureSection load='7s54' size='340' side='right'caption='[[7s54]], [[Resolution|resolution]] 1.79&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[7s54]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7S54 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7S54 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[7s54]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_NCTC_8325 Staphylococcus aureus subsp. aureus NCTC 8325] and [https://en.wikipedia.org/wiki/Streptococcus_agalactiae Streptococcus agalactiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7S54 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7S54 FirstGlance]. <br>
-</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Sortase_A Sortase A], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.70 3.4.22.70] </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]] 1.794&#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=7s54 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7s54 OCA], [https://pdbe.org/7s54 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7s54 RCSB], [https://www.ebi.ac.uk/pdbsum/7s54 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7s54 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/SRTA_STAA8 SRTA_STAA8] Transpeptidase that anchors surface proteins to the cell wall (PubMed:10427003, PubMed:10446208, PubMed:10535938, PubMed:11714722, PubMed:14769030, PubMed:15247224). 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 (PubMed:10446208, PubMed:10535938, PubMed:11714722, PubMed:14769030, PubMed:15247224). This sortase recognizes a Leu-Pro-x-Thr-Gly (LPXTG) motif, which is cleaved by the sortase between the threonine and glycine residues (PubMed:10535938, PubMed:11714722, PubMed:14769030, PubMed:15247224). Utilizes lipid II as the peptidoglycan substrate for the sorting reaction (PubMed:10446208, PubMed:11856734). Responsible for the display of important virulence factors (PubMed:14769030). Important for interactions with the host and host colonization during infection (PubMed:10805806, PubMed:14769030).<ref>PMID:10427003</ref> <ref>PMID:10446208</ref> <ref>PMID:10535938</ref> <ref>PMID:10805806</ref> <ref>PMID:11714722</ref> <ref>PMID:11856734</ref> <ref>PMID:14769030</ref> <ref>PMID:15247224</ref> [https://www.uniprot.org/uniprot/SRTA_STRA3 SRTA_STRA3] Transpeptidase that anchors surface proteins to the cell wall. 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. This sortase recognizes a Leu-Pro-x-Thr-Gly (LPXTG) motif, which is cleaved by the sortase between the threonine and glycine residues (By similarity). Essential for adherence to eukaryotic cells and for binding to fibronectin and fibrinogen (PubMed:15908360).[UniProtKB:Q2FV99]<ref>PMID:15908360</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 23: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Sortase A]]
+[[Category: Staphylococcus aureus subsp. aureus NCTC 8325]]
-[[Category: Amacher, J F]]
+[[Category: Streptococcus agalactiae]]
-[[Category: Antos, J M]]
+[[Category: Amacher JF]]
-[[Category: Gao, M]]
+[[Category: Antos JM]]
-[[Category: Kodama, H M]]
+[[Category: Gao M]]
-[[Category: Eight-stranded beta barrel]]
+[[Category: Kodama HM]]
-[[Category: Housekeeping sortase]]
-[[Category: Hydrolase]]
-[[Category: Sortase]]
-[[Category: Sortase-fold]]
-[[Category: Surface protein]]
-[[Category: Transpeptidase]]

7s54

From Proteopedia

Current revision

Sortase A from Streptococcus agalactiae with the deltaN188 b7-b8 loop sequence from Staphylococcus aureus Sortase A

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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