2BIB

Crystal structure of the complete modular teichioic acid phosphorylcholine esterase Pce (CbpE) from Streptococcus pneumoniae

Summary for 2BIB

• Entry DOI: 10.2210/pdb2bib/pdb
• Descriptor: TEICHOIC ACID PHOSPHORYLCHOLINE ESTERASE/ CHOLINE BINDING PROTEIN, PHOSPHOCHOLINE, 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (6 entities in total)
• Functional Keywords: choline-binding protein, cbpe, pce, phosphorylcholine esterase, hydrolase, teichoic acid
• Biological source: STREPTOCOCCUS PNEUMONIAE
• Total number of polymer chains: 1
• Total formula weight: 65286.88

Authors

Hermoso, J.A.,Lagartera, L.,Gonzalez, A.,Garcia, P.,Martinez-Ripoll, M.,Garcia, J.L.,Menendez, M. (deposition date: 2005-01-20, release date: 2005-05-09, Last modification date: 2024-05-08)

Primary citation

Hermoso, J.A.,Lagartera, L.,Gonzalez, A.,Stelter, M.,Garcia, P.,Martinez-Ripoll, M.,Garcia, J.L.,Menendez, M.
Insights Into Pneumococcal Pathogenesis from Crystal Structure of the Modular Teichoic Acid Phosphorylcholine Esterase Pce
Nat.Struct.Mol.Biol., 12:533-, 2005

PubMed Abstract: Phosphorylcholine, a specific component of the pneumococcal cell wall, is crucial in pathogenesis. It directly binds to the human platelet-activating factor (PAF) receptor and acts as a docking station for the family of surface-located choline-binding proteins (CBP). The first structure of a complete pneumococcal CBP, Pce (or CbpE), has been solved in complex with the reaction product and choline analogs. Pce has a novel modular structure, with a globular N-terminal module containing a binuclear Zn(2+) catalytic center, and an elongated choline-binding module. Residues involved in substrate binding and catalysis are described and modular configuration of the active center accounts for in vivo features of teichoic acid hydrolysis. The hydrolysis of PAF by Pce and its regulatory role in phosphorylcholine decoration of the bacterial surface provide new insights into the critical function of Pce in pneumococcal adherence and invasiveness.

PubMed: 15895092
DOI: 10.1038/NSMB940

Experimental method

X-RAY DIFFRACTION (1.92 Å)