The structure of the cell-wall protease from streptococci that inactivates the human complement factor 5a

C. Kent Brown, Zu Yi Gu, Yury V. Matsuka, Stephen B. Olmsted, P. Patrick Cleary, Douglas H Ohlendorf, Cathleeen A. Earhart

Research output: Contribution to journalArticlepeer-review

Abstract

The structure of a 949-residue fragment of complement factor 5a peptidase (SCP) was determined to 1.9 Å resolution. The molecule is made of five distinct domains in an elongated head-stalk structure. The structure suggests that activity of SCP can be modulated through binding of integrins to 2 RGD sequences. This structure is the first of an enzyme that is covalently attached to the cell wall of a Gram-positive bacteria. SCP is also the first functional protease containing a protease-associated domain to have its structure elucidated.

Original languageEnglish (US)
Pages (from-to)211-215
Number of pages5
JournalInternational Congress Series
Volume1289
DOIs
StatePublished - Apr 1 2006

Keywords

  • Allosteric control
  • Crystal structure
  • Fibronectin
  • Protease-associated domain
  • Serine protease
  • Virulence

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