2bib
From Proteopedia
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| , resolution 1.92Å | |||||||
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| Sites: | |||||||
| Ligands: | , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 role in phosphorylcholine decoration of the bacterial surface provide new insights into the critical function of Pce in pneumococcal adherence and invasiveness.
About this Structure
2BIB is a Single protein structure of sequence from Streptococcus pneumoniae. 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
Page seeded by OCA on Mon Mar 31 02:06:49 2008
