2X8P

Crystal Structure of CbpF in Complex with Atropine by Co- Crystallization

Summary for 2X8P

• Entry DOI: 10.2210/pdb2x8p/pdb
• Related: 2V04 2V05 2VYU 2X8M 2X8O
• Descriptor: CHOLINE-BINDING PROTEIN F, SULFATE ION, (1R,5S)-8-METHYL-8-AZABICYCLO[3.2.1]OCT-3-YL (2R)-3-HYDROXY-2-PHENYLPROPANOATE, ... (6 entities in total)
• Functional Keywords: choline-binding protein, lipid-binding-protein
• Biological source: STREPTOCOCCUS PNEUMONIAE
• Total number of polymer chains: 1
• Total formula weight: 37702.78

Authors

Silva-Martin, N.,Hermoso, J.A. (deposition date: 2010-03-10, release date: 2011-04-06, Last modification date: 2023-12-20)

Primary citation

Silva-Martin, N.,Retamosa, M.G.,Maestro, B.,Bartual, S.G.,Rodes, M.J.,Garcia, P.,Sanz, J.M.,Hermoso, J.A.
Crystal Structures of Cbpf Complexed with Atropine and Ipratropium Reveal Clues for the Design of Novel Antimicrobials Against Streptococcus Pneumoniae.
Biochim.Biophys.Acta, 1840:129-, 2013

PubMed Abstract: Streptococcus pneumoniae is a major pathogen responsible of important diseases worldwide such as pneumonia and meningitis. An increasing resistance level hampers the use of currently available antibiotics to treat pneumococcal diseases. Consequently, it is desirable to find new targets for the development of novel antimicrobial drugs to treat pneumococcal infections. Surface choline-binding proteins (CBPs) are essential in bacterial physiology and infectivity. In this sense, esters of bicyclic amines (EBAs) such as atropine and ipratropium have been previously described to act as choline analogs and effectively compete with teichoic acids on binding to CBPs, consequently preventing in vitro pneumococcal growth, altering cell morphology and reducing cell viability.

PubMed: 24036328
DOI: 10.1016/J.BBAGEN.2013.09.006

Experimental method

X-RAY DIFFRACTION (2.27 Å)