1wra: Difference between revisions

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[[Image:1wra.gif|left|200px]]
{{Seed}}
[[Image:1wra.png|left|200px]]


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{{STRUCTURE_1wra|  PDB=1wra  |  SCENE=  }}  
{{STRUCTURE_1wra|  PDB=1wra  |  SCENE=  }}  


'''Crystal Structure of Phosphorylcholine Esterase Domain of the Virulence Factor Choline Binding Protein E from Streptococcus Pneumoniae'''
===Crystal Structure of Phosphorylcholine Esterase Domain of the Virulence Factor Choline Binding Protein E from Streptococcus Pneumoniae===




==Overview==
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Streptococcus pneumoniae is the worldwide leading cause of deaths from invasive infections such as pneumoniae, sepsis, and meningitidis in children and the elderly. Nasopharyngeal colonization, which plays a key role in the development of pneumococcal disease, is highly dependent on a family of surface-exposed proteins, the choline-binding proteins (CBPs). Here we report the crystal structure of phosphorylcholine esterase (Pce), the catalytic domain of choline-binding protein E (CBPE), which has been shown to be crucial for host/pathogen interaction processes. The unexpected features of the Pce active site reveal that this enzyme is unique among the large family of hydrolases harboring the metallo-beta-lactamase fold. The orientation and calcium stabilization features of an elongated loop, which lies on top of the active site, suggest that the cleft may be rearranged. Furthermore, the structure of Pce complexed with phosphorylcholine, together with the characterization of the enzymatic role played by two iron ions located in the active site allow us to propose a reaction mechanism reminiscent of that of purple acid phosphatase. This mechanism is supported by site-directed mutagenesis experiments. Finally, the interactions of the choline binding domain and the Pce region of CBPE with chains of teichoic acids have been modeled. The ensemble of our biochemical and structural results provide an initial understanding of the function of CBPE.
The line below this paragraph, {{ABSTRACT_PUBMED_15908436}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_15908436}}


==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Crystal structure of phosphorylcholine esterase domain of the virulence factor choline-binding protein e from streptococcus pneumoniae: new structural features among the metallo-beta-lactamase superfamily., Garau G, Lemaire D, Vernet T, Dideberg O, Di Guilmi AM, J Biol Chem. 2005 Aug 5;280(31):28591-600. Epub 2005 May 20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15908436 15908436]
Crystal structure of phosphorylcholine esterase domain of the virulence factor choline-binding protein e from streptococcus pneumoniae: new structural features among the metallo-beta-lactamase superfamily., Garau G, Lemaire D, Vernet T, Dideberg O, Di Guilmi AM, J Biol Chem. 2005 Aug 5;280(31):28591-600. Epub 2005 May 20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15908436 15908436]
Identification of the teichoic acid phosphorylcholine esterase in Streptococcus pneumoniae., Vollmer W, Tomasz A, Mol Microbiol. 2001 Mar;39(6):1610-22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11260477 11260477]
A novel solenoid fold in the cell wall anchoring domain of the pneumococcal virulence factor LytA., Fernandez-Tornero C, Lopez R, Garcia E, Gimenez-Gallego G, Romero A, Nat Struct Biol. 2001 Dec;8(12):1020-4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11694890 11694890]
[[Category: Glycerophosphocholine cholinephosphodiesterase]]
[[Category: Glycerophosphocholine cholinephosphodiesterase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Pneum]]
[[Category: Pneum]]
[[Category: Streptococcus]]
[[Category: Streptococcus]]
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