Structure of the streptococcal cell wall C5a peptidase

被引：55
作者：
Brown, CK
Gu, ZY
Matsuka, YV
Purushothaman, SS
Winter, LA
Cleary, PP
Olmsted, SB
Ohlendorf, DH
Earhart, CA [1 ]
机构：
[1] Univ Minnesota, Dept Biochem, Minneapolis, MN 55455 USA
[2] Univ Minnesota, Dept Mol Biol, Minneapolis, MN 55455 USA
[3] Univ Minnesota, Dept Biophys, Minneapolis, MN 55455 USA
[4] Univ Minnesota, Dept Microbiol, Minneapolis, MN 55455 USA
[5] Wyeth Res, Pearl River, NY 10965 USA
来源：
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2005年 / 102卷 / 51期
关键词：
bacterial adhesins; endopeptidases; molecular models; Streptococcus agalactiae; x-ray crystallography;
D O I：
10.1073/pnas.0504954102
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
The structure of a cell surface enzyme from a Gram-positive pathogen has been determined to 2-angstrom 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 U-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 SCIP binding to integrins by the RGD motifs may stabilize conformational changes required for substrate binding.
引用
收藏
页码：18391 / 18396
页数：6
相关论文
共 39 条
[1]   Processing, stability, and kinetic parameters of C5a peptidase from Streptococcus pyogenes [J].
Anderson, ET ;
Wetherell, MG ;
Winter, LA ;
Olmsted, SB ;
Cleary, PP ;
Matsuka, YV .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 2002, 269 (19) :4839-4851
[2]   Identification of novel adhesins from group B streptococci by use of phage display reveals that C5a peptidase mediates fibronectin binding [J].
Beckmann, C ;
Waggoner, JD ;
Harris, TO ;
Tamura, GS ;
Rubens, CE .
INFECTION AND IMMUNITY, 2002, 70 (06) :2869-2876
[3]   THE HIGH-RESOLUTION X-RAY CRYSTAL-STRUCTURE OF THE COMPLEX FORMED BETWEEN SUBTILISIN CARLSBERG AND EGLIN-C, AN ELASTASE INHIBITOR FROM THE LEECH HIRUDO-MEDICINALIS - STRUCTURAL-ANALYSIS, SUBTILISIN STRUCTURE AND INTERFACE GEOMETRY .2. [J].
BODE, W ;
PAPAMOKOS, E ;
MUSIL, D .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1987, 166 (03) :673-692
[4]   Structure and distribution of modules in extracellular proteins [J].
Bork, P ;
Downing, AK ;
Kieffer, B ;
Campbell, ID .
QUARTERLY REVIEWS OF BIOPHYSICS, 1996, 29 (02) :119-167
[5]   CRYSTALLOGRAPHIC R-FACTOR REFINEMENT BY MOLECULAR-DYNAMICS [J].
BRUNGER, AT ;
KURIYAN, J ;
KARPLUS, M .
SCIENCE, 1987, 235 (4787) :458-460
[6]  
CHEN CC, 1990, J BIOL CHEM, V265, P3161
[7]   The group B streptococcal C5a peptidase is both a specific protease and an invasin [J].
Cheng, Q ;
Stafslien, D ;
Purushothaman, SS ;
Cleary, P .
INFECTION AND IMMUNITY, 2002, 70 (05) :2408-2413
[8]   Structure of the human transferrin receptor-transferrin complex [J].
Cheng, Y ;
Zak, O ;
Alsen, P ;
Harrison, SC ;
Walz, T .
CELL, 2004, 116 (04) :565-576
[9]   Immunization with C5a peptidase from either group A or B streptococci enhances clearance of group A streptococci from intranasally infected mice [J].
Cleary, PP ;
Matsuka, YV ;
Huynh, T ;
Lam, H ;
Olmsted, SB .
VACCINE, 2004, 22 (31-32) :4332-4341
[10]  
CLEARY PP, 1998, HDB PROTEOLYTIC ENZY, P308
1234