Student or educator? Sign up with your school email and get 6 months of Pro free.
CoChat
Sign Up
Cited by 269

The DOI matches its Crossref record; 16 of the 16 references it cites were found in a registry or an index.

Crystal Structures of Staphylococcus aureus Sortase A and Its Substrate Complex

Open access
Zong, Yinong, Bice, Todd W., Ton-That, Hung, Schneewind, Olaf, Narayana, Sthanam V.L.·2004·Journal of Biological Chemistry
DOI 10.1074/jbc.m401374200
Open this paper in CoChat — free account

Abstract

The cell wall envelope of staphylococci and other Gram-positive pathogens is coated with surface proteins that interact with human host tissues. Surface proteins of Staphylococcus aureus are covalently linked to the cell wall envelope by a mechanism requiring C-terminal sorting signals with an LPXTG motif. Sortase (SrtA) cleaves surface proteins between the threonine (T) and the glycine (G) of the LPXTG motif and catalyzes the formation of an amide bond between threonine at the C-terminal end of polypeptides and cell wall cross-bridges. The active site architecture and catalytic mechanism of sortase A has hitherto not been revealed. Here we present the crystal structures of native SrtA, of an active site mutant of SrtA, and of the mutant SrtA complexed with its substrate LPETG peptide and describe the substrate binding pocket of the enzyme. Highly conserved proline (P) and threonine (T) residues of the LPXTG motif are held in position by hydrophobic contacts, whereas the glutamic acid residue (E) at the X position points out into the solvent. The scissile T-G peptide bond is positioned between the active site Cys(184) and Arg(197) residues and at a greater distance from the imidazolium side chain of His(120). All three residues, His(120), Cys(184), and Arg(197), are conserved in sortase enzymes from Gram-positive bacteria. Comparison of the active sites of S. aureus sortase A and sortase B provides insight into substrate specificity and suggests a universal sortase-catalyzed mechanism of bacterial surface protein anchoring in Gram-positive bacteria.

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1074/jbc.m401374200

Cites

16 of 16 references verified0 citation errors · 0 not checkable

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Show all 16 references

Research works printed but not linked: 35

  1. Foster, 1998, Trends Microbiol., 6, 484, 10.1016/S0966-842X(98)01400-0 · DOI · Paper page
  2. Navarre, 1999, Microbiol. Mol. Biol. Rev., 63, 174, 10.1128/MMBR.63.1.174-229.1999 · DOI · Paper page
  3. Mazmanian, 2000, Proc. Natl. Acad. Sci. U. S. A., 97, 5510, 10.1073/pnas.080520697 · DOI · Paper page
  4. Navarre, 1994, Mol. Microbiol., 14, 115, 10.1111/j.1365-2958.1994.tb01271.x · DOI · Paper page
  5. Schneewind, 1995, Science, 268, 103, 10.1126/science.7701329 · DOI · Paper page
  6. Ton-That, 1998, J. Biol. Chem., 273, 29143, 10.1074/jbc.273.44.29143 · DOI
  7. Kruger, 2004, Biochemistry, 43, 1541, 10.1021/bi035920j · DOI
  8. Jonsson, 2002, J. Infect. Dis., 185, 1417, 10.1086/340503 · DOI · Paper page
  9. Jonsson, 2003, Microb. Infect., 5, 775, 10.1016/S1286-4579(03)00143-6 · DOI
  10. Pallen, 2001, Trends Microbiol., 9, 97, 10.1016/S0966-842X(01)01956-4 · DOI · Paper page
  11. Bolken, 2001, Infect. Immun., 69, 75, 10.1128/IAI.69.1.75-80.2001 · DOI
  12. Kharat, 2003, Infect. Immun., 71, 2758, 10.1128/IAI.71.5.2758-2765.2003 · DOI
  13. Hava, 2003, J. Bacteriol., 185, 413, 10.1128/JB.185.2.413-421.2003 · DOI
  14. Lee, 2003, Infect. Immun., 71, 676, 10.1128/IAI.71.2.676-681.2003 · DOI
  15. Bierne, 2002, Mol. Microbiol., 43, 869, 10.1046/j.1365-2958.2002.02798.x · DOI · Paper page
  16. Garandeau, 2002, Infect. Immun., 70, 1382, 10.1128/IAI.70.3.1382-1390.2002 · DOI
  17. Ton-That, 1999, J. Biol. Chem., 274, 24316, 10.1074/jbc.274.34.24316 · DOI · Paper page
  18. Ton-That, 2000, J. Biol. Chem., 275, 9876, 10.1074/jbc.275.13.9876 · DOI · Paper page
  19. Doublie, 1997, Methods Enzymol., 276, 523, 10.1016/S0076-6879(97)76075-0 · DOI · Paper page
  20. Otwinowski, 1997, Methods Enzymol., 276, 307, 10.1016/S0076-6879(97)76066-X · DOI · Paper page
  21. Brunger, 1998, Acta Crystallogr. Sect. D Biol. Crystallogr., 54, 905, 10.1107/S0907444998003254 · DOI · Paper page
  22. Riedl, 2001, Cell, 104, 791, 10.1016/S0092-8674(01)00274-4 · DOI
  23. Kamphuis, 1985, J. Mol. Biol., 182, 317, 10.1016/0022-2836(85)90348-1 · DOI · Paper page
  24. Kamphuis, 1984, J. Mol. Biol., 179, 233, 10.1016/0022-2836(84)90467-4 · DOI
  25. Harrison, 1997, J. Am. Chem. Soc., 119, 12285, 10.1021/ja9711472 · DOI
  26. Storer, 1994, Methods Enzymol., 244, 486, 10.1016/0076-6879(94)44035-2 · DOI · Paper page
  27. Paetzel, 1998, Nature, 396, 186, 10.1038/24196 · DOI
  28. Silvaggi, 2003, Biochemistry, 42, 1199, 10.1021/bi0268955 · DOI
  29. Huang, 2003, Biochemistry, 42, 11307, 10.1021/bi034391g · DOI · Paper page
  30. Chai, 2001, Cell, 104, 769, 10.1016/S0092-8674(01)00272-0 · DOI
  31. Pinitglang, 1997, Biochemistry, 36, 9968, 10.1021/bi9705974 · DOI
  32. Dardenne, 2003, Proteins, 52, 236, 10.1002/prot.10368 · DOI
  33. Dessen, 2004, Structure, 12, 6, 10.1016/j.str.2003.12.009 · DOI
  34. Antosiewicz, 1996, J. Comput. Chem., 17, 1633, 10.1002/(SICI)1096-987X(19961115)17:14<1633::AID-JCC5>3.0.CO;2-M · DOI
  35. Burton, 1998, Faraday Discuss., 110, 463, 10.1039/a801719k · DOI

Cited by

Metadata

Authors
Zong, Y., Bice, T. W., Ton-That, H., Schneewind, O., & Narayana, S. V. L.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2004-07
Volume
279
Issue
30
Pages
31383-31389
ISSN
0021-9258 (ISSN-L)
DOI
10.1074/jbc.m401374200
OpenAlex
W2012772141
Cited by
269
References
16
FWCI
2.19
Type
journal article
Language
en
Open access
hybrid
Licence

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.