The Structure of Sortase B, a Cysteine Transpeptidase that Tethers Surface Protein to the Staphylococcus aureus Cell Wall
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Many surface proteins of Gram-positive bacteria, which play important roles during the pathogenesis of human infections, are anchored to the cell wall envelope by a mechanism requiring sortases. Sortase B, a cysteine transpeptidase from Staphylococcus aureus, cleaves the C-terminal sorting signal of IsdC at the NPQTN motif and tethers the polypeptide to the pentaglycine cell wall cross-bridge. During catalysis, the active site cysteine of sortase and the cleaved substrate form an acyl intermediate, which is then resolved by the amino group of pentaglycine cross-bridges. We report here the crystal structures of SrtBDeltaN30 in complex with two active site inhibitors, MTSET and E64, and with the cell wall substrate analog tripleglycine. These structures reveal, for the first time, the active site disposition and the unique Cys-Arg catalytic machinery of the cysteine transpeptidase, and they also provide useful information for the future design of anti-infective agents against sortases.
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The X-ray structure of S. aureus sortase B revealed the presence of an arginine residue in the near vicinity of the catalytic cysteine which is highly conserved among all sortases.
“Recently, the X-ray structure of S. aureus sortase B revealed the presence of an arginine residue in the near vicinity of the catalytic cysteine which is highly conserved among all sortases [45].”
From Protein sorting to the cell wall envelope of Gram-positive bacteria (2004) · cites this paper as [45]
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“…of intestinal fucosyl glycans by C. perfringens (Fan et al., 2016) and sortase B (SrtB), a cysteine transpeptidase has been identified in Staphylococcus aureus that attaches a polypeptide involved in heme iron transport and thus help in iron acquisition during infection (Zong et al., 2004).”
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“…our methodology, we predicted orientations of mC223 in a cysteine transpeptidase, Sortase B. Comparison of the lowest energy orientation and the x-ray structure (Zong et al., 2004) shows that the ammonium nitrogen of mC223 in the model is just 0.66 Å away from the experimental position (Fig.”
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Staphylococcal Sortases and Surface Proteins
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A New Catalytic Dyad Regulates Anchoring of Molecules to the Gram-Positive Cell Wall by Sortases
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“…species: B. anthracis (baSrtB; PDB IDs 1RZ2, 2OQW) (49, 50), C. dif fi cile SrtB (cdSrtB; 4UX7) (38), Clostridium perfringens SrtB (cpSrtB; 5B23, 5YFK) (51), L. monocytogenes (lmSrtB; 5JCV), S. aureus SrtB (saSrtB; 1NG5, 1QWZ, 1QX6, 1QXA, 4LFD) (28, 31), and S. pyogenes SrtB (spySrtB; 3PSQ) (36).”
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- Authors
- Zong, Y., Mazmanian, S. K., Schneewind, O., & Narayana, S. V. L.
- Affiliations
- University of Alabama at Birmingham (US)
- University of Chicago (US)
- Corresponding author
- Narayana, Sthanam V.L
- Venue
- Structure
- Publisher
- Elsevier BV
- Published
- 2004-03
- Volume
- 12
- Issue
- 1
- Pages
- 105-112
- ISSN
- 0969-2126 (ISSN-L)
- OpenAlex
- W1992162955
- Cited by
- 91
- References
- 39
- Citations by year
- 2026: 3 · 2025: 6 · 2024: 1 · 2022: 2 · 2021: 2 · 2020: 4 · 2019: 3 · 2018: 4 · 2017: 4 · 2016: 5 · 2015: 6 · 2014: 9 · 2013: 6 · 2012: 2
- FWCI
- 1.66
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Structure (publishedVersion)
- PubMed (publishedVersion)
- CaltechAUTHORS (California Institute of Technology) (submittedVersion)
- Funders
- National Aeronautics and Space Administration
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
- Health Sciences › Medicine › Infectious Diseases › Antimicrobial Resistance in Staphylococcus
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Keywords
- Staphylococcus aureus, cell wall anchoring, IsdC, active-site-directed inhibitors, MTSET, E-64, crystal structure
- MeSH terms
- Amino Acid Sequence, Anti-Infective Agents, Bacterial Proteins, Cell Wall, Cysteine, Cysteine Endopeptidases, Enzyme Inhibitors, Glycine, Mesylates, Molecular Sequence Data, Peptidyl Transferases, Staphylococcus aureus, Protein Structure, Tertiary, Aminoacyltransferases, Amino Acid Motifs, Protein Transport
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