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

doi:10.1016/j.ics.2005.11.004

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

Structural Biology and Biophysics (TMED)

Research output: Contribution to journal › Article › peer-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 language	English (US)
Pages (from-to)	211-215
Number of pages	5
Journal	International Congress Series
Volume	1289
DOIs	https://doi.org/10.1016/j.ics.2005.11.004
State	Published - Apr 2006

Keywords

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

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10.1016/j.ics.2005.11.004

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

abstract = "The structure of a 949-residue fragment of complement factor 5a peptidase (SCP) was determined to 1.9 {\AA} 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.",

keywords = "Allosteric control, Crystal structure, Fibronectin, Protease-associated domain, Serine protease, Virulence",

author = "Brown, \{C. Kent\} and Gu, \{Zu Yi\} and Matsuka, \{Yury V.\} and Olmsted, \{Stephen B.\} and Cleary, \{P. Patrick\} and Ohlendorf, \{Douglas H\} and Earhart, \{Cathleeen A.\}",

year = "2006",

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doi = "10.1016/j.ics.2005.11.004",

language = "English (US)",

volume = "1289",

pages = "211--215",

journal = "International Congress Series",

issn = "0531-5131",

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T1 - The structure of the cell-wall protease from streptococci that inactivates the human complement factor 5a

AU - Brown, C. Kent

AU - Gu, Zu Yi

AU - Matsuka, Yury V.

AU - Olmsted, Stephen B.

AU - Cleary, P. Patrick

AU - Ohlendorf, Douglas H

AU - Earhart, Cathleeen A.

PY - 2006/4

Y1 - 2006/4

N2 - 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.

AB - 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.

KW - Allosteric control

KW - Crystal structure

KW - Fibronectin

KW - Protease-associated domain

KW - Serine protease

KW - Virulence

UR - https://www.scopus.com/pages/publications/33645927319

UR - https://www.scopus.com/pages/publications/33645927319#tab=citedBy

U2 - 10.1016/j.ics.2005.11.004

DO - 10.1016/j.ics.2005.11.004

M3 - Article

AN - SCOPUS:33645927319

SN - 0531-5131

VL - 1289

SP - 211

EP - 215

JO - International Congress Series

JF - International Congress Series

ER -

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

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