The Structure of the Cell-Wall Protease from Streptococci that Inactivates the Human Complement Factor 5A

Journal Article · Sun Jan 01 00:00:00 EST 2006 · Int. Congr. Ser.

DOI:https://doi.org/10.1016/j.ics.2005.11.004· OSTI ID:914264

Brown, C; Gu, Z; Matsuka, Y; Olmsted, S; Cleary, P; Ohlendorf, D; Earhart, C

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.

• Research Organization: Brookhaven National Lab. (BNL), Upton, NY (United States). National Synchrotron Light Source
• Sponsoring Organization: Doe - Office Of Science
• DOE Contract Number: DE-AC02-98CH10886
• OSTI ID: 914264
• Report Number(s): BNL-78832-2007-JA; TRN: US200809%%125
• Journal Information: Int. Congr. Ser., Vol. 1289
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
BACTERIA
CELL WALL
ENZYMES
FUNCTIONALS
RESOLUTION
PROTEIN STRUCTURE
national synchrotron light source