2v05

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{{STRUCTURE_2v05| PDB=2v05 | SCENE= }}
{{STRUCTURE_2v05| PDB=2v05 | SCENE= }}
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'''CRYSTAL STRUCTURE OF CHOLINE BINDING PROTEIN F FROM STREPTOCOCCUS PNEUMONIAE. CRYSTAL FORM II.'''
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===CRYSTAL STRUCTURE OF CHOLINE BINDING PROTEIN F FROM STREPTOCOCCUS PNEUMONIAE. CRYSTAL FORM II.===
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==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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15908436 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15908436}}
==About this Structure==
==About this Structure==
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[[Category: Choline-binding-protein]]
[[Category: Choline-binding-protein]]
[[Category: Lipid-binding-protein]]
[[Category: Lipid-binding-protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 11 10:44:58 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:14:36 2008''

Revision as of 16:14, 27 July 2008

Image:2v05.png

Template:STRUCTURE 2v05

CRYSTAL STRUCTURE OF CHOLINE BINDING PROTEIN F FROM STREPTOCOCCUS PNEUMONIAE. CRYSTAL FORM II.

Template:ABSTRACT PUBMED 15908436

About this Structure

2V05 is a Single protein structure of sequence from Streptococcus pneumoniae. Full crystallographic information is available from OCA.

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:15908436

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