2bib
From Proteopedia
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CRYSTAL STRUCTURE OF THE COMPLETE MODULAR TEICHIOIC ACID PHOSPHORYLCHOLINE ESTERASE PCE (CBPE) FROM STREPTOCOCCUS PNEUMONIAE
Overview
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 ... [(full description)]
About this Structure
2BIB is a [Single protein] structure of sequence from [Streptococcus pneumoniae] with ZN, CA, PC and BTB as [ligands]. Full crystallographic information is available from [OCA].
Reference
Insights into pneumococcal pathogenesis from the crystal structure of the modular teichoic acid phosphorylcholine esterase Pce., Hermoso JA, Lagartera L, Gonzalez A, Stelter M, Garcia P, Martinez-Ripoll M, Garcia JL, Menendez M, Nat Struct Mol Biol. 2005 Jun;12(6):533-8. Epub 2005 May 15. PMID:15895092
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