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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 Angstroms 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.

Authors:
; ; ; ; ; ;
Publication Date:
Research Org.:
Brookhaven National Laboratory (BNL) National Synchrotron Light Source
Sponsoring Org.:
Doe - Office Of Science
OSTI Identifier:
914264
Report Number(s):
BNL-78832-2007-JA
TRN: US200809%%125
DOE Contract Number:  
DE-AC02-98CH10886
Resource Type:
Journal Article
Resource Relation:
Journal Name: Int. Congr. Ser.; Journal Volume: 1289
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; BACTERIA; CELL WALL; ENZYMES; FUNCTIONALS; RESOLUTION; PROTEIN STRUCTURE; national synchrotron light source

Citation Formats

Brown,C., Gu, Z., Matsuka, Y., Olmsted, S., Cleary, P., Ohlendorf, D., and Earhart, C. The Structure of the Cell-Wall Protease from Streptococci that Inactivates the Human Complement Factor 5A. United States: N. p., 2006. Web. doi:10.1016/j.ics.2005.11.004.
Brown,C., Gu, Z., Matsuka, Y., Olmsted, S., Cleary, P., Ohlendorf, D., & Earhart, C. The Structure of the Cell-Wall Protease from Streptococci that Inactivates the Human Complement Factor 5A. United States. doi:10.1016/j.ics.2005.11.004.
Brown,C., Gu, Z., Matsuka, Y., Olmsted, S., Cleary, P., Ohlendorf, D., and Earhart, C. Sun . "The Structure of the Cell-Wall Protease from Streptococci that Inactivates the Human Complement Factor 5A". United States. doi:10.1016/j.ics.2005.11.004.
@article{osti_914264,
title = {The Structure of the Cell-Wall Protease from Streptococci that Inactivates the Human Complement Factor 5A},
author = {Brown,C. and Gu, Z. and Matsuka, Y. and Olmsted, S. and Cleary, P. and Ohlendorf, D. and Earhart, C.},
abstractNote = {The structure of a 949-residue fragment of complement factor 5a peptidase (SCP) was determined to 1.9 Angstroms 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.},
doi = {10.1016/j.ics.2005.11.004},
journal = {Int. Congr. Ser.},
number = ,
volume = 1289,
place = {United States},
year = {Sun Jan 01 00:00:00 EST 2006},
month = {Sun Jan 01 00:00:00 EST 2006}
}