 |
InterPro: IPR018337 Cell wall/choline-binding repeat
Protein matches
|
UniProtKB Matches: 1661 proteins |
|
Accession
|
IPR018337 Cell_wall/Cho-bd_repeat |
Type
|
Repeat |
Signatures
|
|
InterPro Relationships
|
|
Children
|
IPR002479 Putative cell wall binding repeat
|
|
InterPro annotation
|
|
Entry Details in BioMart
|
Abstract
|
The cell wall-binding repeat (CW) is an about 20 amino acid residue module, essentially found in two bacterial Gram-positive protein families; the choline binding proteins and glucosyltransferases (EC:2.4.1.5). In choline-binding proteins cell wall binding repeats bind to choline moieties of both teichoic and lipoteichoic acids, two components peculiar to the cell surface of Gram-positive bacteria [1, 2]. In glucosyltransferases the region spanning the CW repeats is a glucan binding domain [3].
Several crystal structures of CW have been solved [4, 5]. In the choline binding protein LytA, the repeats adopt a solenoid fold consisting exclusively of beta-hairpins that stack to form a left-handed superhelix with a boomerang-like shape. The choline groups bind between beta-hairpin 'steps' of the superhelix [4]. In Cpl-1 CW repeats assemble in two sub-domains: an N-terminal superhelical moiety similar to the LytA one and a C-terminal beta-sheet involved in interactions with the lysozyme domain. Choline is bound between repeats 1 and 2, and, 2 and 3 of the superhelical sub-domain [5].
Some proteins known to contain cell-wall binding repeats include:
- Pneumococcal N-acetylmuramoyl-L-alanine amidase (autolysin, lytA) (EC:3.5.1.28). It is a surface-exposed enzyme that rules the self-destruction of pneumococcal cells through degradation of their peptidoglycan backbone. It mediates the release of toxic substances that damage the host tissues.
- Pneumococcal endo-beta-N-acetylglucosaminidase (lytB) (EC:3.2.1.96). It plays an important role in cell wall degradation and cell separation.
- Pneumococcal teichoic acid phosphorylcholine esterase (pce or cbpE), a cell wall hydrolase important for cellular adhesion and colonisation.
- Lactobacillales glucosyltransferase. It catalyses the transfer of glucosyl units from the cleavage of sucrose to a growing chain of glucan.
- Clostridium difficile toxin A (tcdA) and toxin B (tcdb). They are the causative agents of the antibiotic-associated pseudomembranous colitis. They are intracellular acting toxins that reach their targets after receptor-mediated endocytosis.
- Clostridium acetobutylicum cspA protein.
- Siphoviridae bacteriophages N-acetylmuramoyl-L-alanine amidase. It lyses the bacterial host cell wall.
- Podoviridae lysozyme protein (cpl-1). It is capable of digesting the pneumococcal cell wall.
The cell wall binding repeats are also known as the choline-binding repeats (ChBr) or the choline-binding domain (ChBD).
|
Structural links
|
|
Publications
|
|
1.
|
Garcia-Bustos JF, Tomasz A.
Teichoic acid-containing muropeptides from Streptococcus pneumoniae as substrates for the pneumococcal autolysin.
J. Bacteriol. 169 447-53 1987
[PubMed: 2879828]
http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=2879828&action=stream&blobtype=pdf
|
|
2.
|
Lopez R, Garcia E.
Recent trends on the molecular biology of pneumococcal capsules, lytic enzymes, and bacteriophage.
FEMS Microbiol. Rev. 28 553-80 2004
[PubMed: 15539074]
http://dx.doi.org/10.1016/j.femsre.2004.05.002
|
|
3.
|
Shah DS, Joucla G, Remaud-Simeon M, Russell RR.
Conserved repeat motifs and glucan binding by glucansucrases of oral streptococci and Leuconostoc mesenteroides.
J. Bacteriol. 186 8301-8 2004
[PubMed: 15576779]
http://dx.doi.org/10.1128/JB.186.24.8301-8308.2004
|
|
4.
|
Fernandez-Tornero C, Lopez R, Garcia E, Gimenez-Gallego G, Romero A.
A novel solenoid fold in the cell wall anchoring domain of the pneumococcal virulence factor LytA.
Nat. Struct. Biol. 8 1020-4 2001
[PubMed: 11694890]
http://dx.doi.org/10.1038/nsb724
|
|
5.
|
Hermoso JA, Monterroso B, Albert A, Galan B, Ahrazem O, Garcia P, Martinez-Ripoll M, Garcia JL, Menendez M.
Structural basis for selective recognition of pneumococcal cell wall by modular endolysin from phage Cp-1.
Structure 11 1239-49 2003
[PubMed: 14527392]
http://dx.doi.org/10.1016/j.str.2003.09.005
|
Additional Reading
|
|
Hermoso JA, Lagartera L, Gonzalez A, Stelter M, Garcia P, Martinez-Ripoll M, Garcia JL, Menendez M.
Insights into pneumococcal pathogenesis from the crystal structure of the modular teichoic acid phosphorylcholine esterase Pce.
Nat. Struct. Mol. Biol. 12 2005 533-8
[PubMed: 15895092]
http://dx.doi.org/10.1038/nsmb940
|
|
Fernandez-Tornero C, Garcia E, Lopez R, Gimenez-Gallego G, Romero A.
Two new crystal forms of the choline-binding domain of the major pneumococcal autolysin: insights into the dynamics of the active homodimer.
J. Mol. Biol. 321 2002 163-73
[PubMed: 12139941]
http://dx.doi.org/10.1016/S0022-2836(02)00596-X
|
|
Perez-Dorado I, Campillo NE, Monterroso B, Hesek D, Lee M, Paez JA, Garcia P, Martinez-Ripoll M, Garcia JL, Mobashery S, Menendez M, Hermoso JA.
Elucidation of the molecular recognition of bacterial cell wall by modular pneumococcal phage endolysin CPL-1.
J. Biol. Chem. 282 2007 24990-9
[PubMed: 17581815]
http://dx.doi.org/10.1074/jbc.M704317200
|
|
Fernandez-Tornero C, Garcia E, de Pascual-Teresa B, Lopez R, Gimenez-Gallego G, Romero A.
Ofloxacin-like antibiotics inhibit pneumococcal cell wall-degrading virulence factors.
J. Biol. Chem. 280 2005 19948-57
[PubMed: 15769740]
http://dx.doi.org/10.1074/jbc.M501236200
|
|
|
InterPro 23.1
|