2v05
From Proteopedia
(New page: '''Unreleased structure''' The entry 2v05 is ON HOLD until Paper Publication Authors: Hermoso, J., Molina, R., Kahn, R., Stelter, M. Description: CRYSTAL STRUCTURE OF CHOLINE BINDING P...) |
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| + | {{STRUCTURE_2v05| PDB=2v05 | SCENE= }} | ||
| - | + | '''CRYSTAL STRUCTURE OF CHOLINE BINDING PROTEIN F FROM STREPTOCOCCUS PNEUMONIAE. CRYSTAL FORM II.''' | |
| - | Description: CRYSTAL STRUCTURE OF CHOLINE BINDING PROTEIN F FROM STREPTOCOCCUS PNEUMONIAE. CRYSTAL FORM II. | ||
| + | ==Overview== | ||
| + | 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. | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 11 | + | ==About this Structure== |
| + | 2V05 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V05 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:[http://www.ncbi.nlm.nih.gov/pubmed/15908436 15908436] | ||
| + | [[Category: Single protein]] | ||
| + | [[Category: Streptococcus pneumoniae]] | ||
| + | [[Category: Hermoso, J.]] | ||
| + | [[Category: Kahn, R.]] | ||
| + | [[Category: Molina, R.]] | ||
| + | [[Category: Stelter, M.]] | ||
| + | [[Category: Cbpf]] | ||
| + | [[Category: Choline-binding-protein]] | ||
| + | [[Category: Lipid-binding-protein]] | ||
| + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 11 10:44:58 2008'' | ||
Revision as of 07:44, 11 June 2008
CRYSTAL STRUCTURE OF CHOLINE BINDING PROTEIN F FROM STREPTOCOCCUS PNEUMONIAE. CRYSTAL FORM II.
Overview
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.
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 Page seeded by OCA on Wed Jun 11 10:44:58 2008
