2bib
From Proteopedia
| Line 5: | Line 5: | ||
==Overview== | ==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 . | + | 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== | ==About this Structure== | ||
| - | 2BIB is a | + | 2BIB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae] with ZN, CA, PC and BTB as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BIB OCA]. |
==Reference== | ==Reference== | ||
| Line 32: | Line 32: | ||
[[Category: teichoic acid]] | [[Category: teichoic acid]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 15:22:06 2007'' |
Revision as of 13:16, 5 November 2007
|
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 with ZN, CA, PC and BTB as ligands. Structure known Active Site: AC1. 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 Nov 5 15:22:06 2007
