Cited by 71Biochemical and Structural CharacterizationStreptococcal Infections and TreatmentsEnzyme Structure and Function

Structure of the streptococcal cell wall C5a peptidase.

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Brown, C. Kent, Gu, Zu-Yi, Matsuka, Yury V., Purushothaman, Sai S., Winter, Laurie A., Cleary, P. Patrick, Olmsted, Stephen B., Ohlendorf, Douglas H. +1 more·2005·Proceedings of the National Academy of Sciences

Abstract

The structure of a cell surface enzyme from a gram-positive pathogen has been determined to 2-A resolution. Gram-positive pathogens have a thick cell wall to which proteins and carbohydrate are covalently attached. Streptococcal C5a peptidase (SCP), is a highly specific protease and adhesin/invasin. Structural analysis of a 949-residue fragment of the [D130A,S512A] mutant of SCP from group B Streptococcus (S. agalactiae, SCPB) revealed SCPB is composed of five distinct domains. The N-terminal subtilisin-like protease domain has a 134-residue protease-associated domain inserted into a loop between two beta-strands. This domain also contains one of two Arg-Gly-Asp (RGD) sequences found in SCPB. At the C terminus are three fibronectin type III (Fn) domains. The second RGD sequence is located between Fn1 and Fn2. Our analysis suggests that SCP binding to integrins by the RGD motifs may stabilize conformational changes required for substrate binding.

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  • The structure determined by Brown et al. (2005) was obtained with a recombinant mutant protein expressed in E. coli with the asp and ser of catalytic triad replaced by alanines and without pro-peptide; this structure has the histidine of catalytic triad separated by 20 Å from active position.

    “The structure determined by Brown et al. (2005) was obtained with a recombinant mutant protein expressed in Escherichia coli with the asp and ser of the catalytic triad replaced by alanines and without the pro-peptide. This structure has the histidine of the catalytic triad separated by 20 Å from the active position (Brown et al., 2005).”

    From Modeled Structure of the Cell Envelope Proteinase of Lactococcus lactis (2020) · cites this paper as Brown et al., 2005

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Research works printed but not linked: 2

  1. Cleary, P. P., Matsuka, Y. V., Huynh, T., Lam, H. & Olmsted, S. B. (2004) Vaccine 22, 5332–5341.
  2. Dauter, Z., Betzel, C., Genov, N., Pipon, N. & Wilson, K. S. (1991) Acta Crystallogr. B 47, 707–730.1793542

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Authors
Brown, C. K., Gu, Z.-Y., Matsuka, Y. V., Purushothaman, S. S., Winter, L. A., Cleary, P. P., Olmsted, S. B., Ohlendorf, D. H., & Earhart, C. A.
Affiliations
University of Minnesota (US)
Venue
Proceedings of the National Academy of Sciences
Published
2005-12-12
Volume
102
Issue
51
Pages
18391-18396
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2135032011
Cited by
70
References
39
Citations by year
2026: 2 · 2025: 1 · 2024: 2 · 2023: 5 · 2022: 2 · 2021: 5 · 2020: 6 · 2019: 2 · 2018: 5 · 2017: 2 · 2016: 2 · 2015: 1 · 2014: 6 · 2013: 2 · 2012: 3
FWCI
0.82
Type
journal article
Language
en
Open access
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • University of Minnesota
  • National Institutes of Health
  • National Institute on Aging (R01AG050607)
  • National Institute of Allergy and Infectious Diseases (R01AI020016, R01 AI50607, R01AI057585)
  • Brookhaven National Laboratory
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
  • Health Sciences › Medicine › Public Health, Environmental and Occupational Health › Streptococcal Infections and Treatments
  • Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
Keywords
protein structure, RGD motif, integrin binding, fibronectin type III domain, adhesins, conformational change, substrate binding, Gram-positive bacterial cell wall
MeSH terms
Amino Acid Sequence, Cell Wall, Models, Molecular, Endopeptidases, Protein Binding, Streptococcus agalactiae, Protein Structure, Tertiary, Crystallography, X-Ray, Adhesins, Bacterial, Amino Acid Motifs, Protein Structure, Quaternary

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