The structural basis of receptor-binding by Escherichia coli associated with diarrhea and septicemia

被引：34
作者：
Merckel, MC
Tanskanen, J
Edelman, S
Westerlund-Wikström, B
Korhonen, TK
Goldman, A
机构：
[1] Univ Helsinki, Viikki Bioctr, Inst Biotechnol, FIN-00014 Helsinki, Finland
[2] Univ Helsinki, Viikki Bioctr, Dept Biosci, Div Gen Microbiol, FIN-00014 Helsinki, Finland
来源：
JOURNAL OF MOLECULAR BIOLOGY | 2003年 / 331卷 / 04期
基金：
芬兰科学院;
关键词：
X-ray crystallography; protein function; protein evolution;
D O I：
10.1016/S0022-2836(03)00841-6
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
GafD in Escherichia coli G (F17) fimbriae is associated with diarrheal disease, and the structure of the ligand-binding domain, GafD1-178, has been determined at 1.7 Angstrom resolution in the presence of the receptor sugar N-acetyl-D-glucosamine. The overall fold is a beta-barrel jelly-roll fold. The ligand-binding site was identified and localized to the side of the molecule. Receptor binding is mediated by side-chain as well main-chain interactions. Ala43-Asn44, Ser116-Thr117 form the sugar acetamide specificity pocket, while Asp88 confers tight binding and Trp109 appears to position the ligand. There is a disulfide bond that rigidifies the acetamide specificity pocket. The three fimbrial lectins, GafD, FimH and PapG share similar beta-barrel folds but display different ligand-binding regions and disulfide-bond patterns. We suggest an evolutionary path for the evolution of the very diverse fimbrial lectins from a common ancestral fold. (C) 2003 Elsevier Ltd. All rights reserved.
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收藏
页码：897 / 905
页数：9
相关论文
共 44 条
[1]   THE CCP4 SUITE - PROGRAMS FOR PROTEIN CRYSTALLOGRAPHY [J].
BAILEY, S .
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1994, 50 :760-763
[2]   Functions of cell surface heparan sulfate proteoglycans [J].
Bernfield, M ;
Götte, M ;
Park, PW ;
Reizes, O ;
Fitzgerald, ML ;
Lincecum, J ;
Zako, M .
ANNUAL REVIEW OF BIOCHEMISTRY, 1999, 68 :729-777
[3]   Crystallography & NMR system:: A new software suite for macromolecular structure determination [J].
Brunger, AT ;
Adams, PD ;
Clore, GM ;
DeLano, WL ;
Gros, P ;
Grosse-Kunstleve, RW ;
Jiang, JS ;
Kuszewski, J ;
Nilges, M ;
Pannu, NS ;
Read, RJ ;
Rice, LM ;
Simonson, T ;
Warren, GL .
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1998, 54 :905-921
[4]   Mutational analysis of receptor binding mediated by the Dr family of Escherichia coli adhesins [J].
Carnoy, C ;
Moseley, SL .
MOLECULAR MICROBIOLOGY, 1997, 23 (02) :365-379
[5]  
Charm S. E., 1971, METHOD ENZYMOL, V22, P476
[6]   X-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli [J].
Choudhury, D ;
Thompson, A ;
Stojanoff, V ;
Langermann, S ;
Pinkner, J ;
Hultgren, SJ ;
Knight, SD .
SCIENCE, 1999, 285 (5430) :1061-1066
[7]   ADDITIVE PROTECTIVE EFFECTS OF COLOSTRAL ANTIPILI ANTIBODIES IN CALVES EXPERIMENTALLY INFECTED WITH ENTERO-TOXIGENIC ESCHERICHIA-COLI [J].
CONTREPOIS, MG ;
GIRARDEAU, JP .
INFECTION AND IMMUNITY, 1985, 50 (03) :947-949
[8]   Modified phased translation functions and their application to molecular-fragment location [J].
Cowtan, K .
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1998, 54 :750-756
[9]   Phase combination and cross validation in iterated density-modification calculations [J].
Cowtan, KD ;
Main, P .
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1996, 52 :43-48
[10]   Structural basis of the interaction of the pyelonephritic E. coli adhesin to its human kidney receptor [J].
Dodson, KW ;
Pinkner, JS ;
Rose, T ;
Magnusson, G ;
Hultgren, SJ ;
Waksman, G .
CELL, 2001, 105 (06) :733-743
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