4B6G

The Crystal Structure of the Neisserial Esterase D.

Summary for 4B6G

• Entry DOI: 10.2210/pdb4b6g/pdb
• Descriptor: PUTATIVE ESTERASE (2 entities in total)
• Functional Keywords: hydrolase, formaldehyde detoxification, alpha/beta serine hydrolase
• Biological source: NEISSERIA MENINGITIDIS MC58
• Total number of polymer chains: 2
• Total formula weight: 64776.39

Authors

Counago, R.M.,Kobe, B. (deposition date: 2012-08-13, release date: 2012-11-14, Last modification date: 2023-12-20)

Primary citation

Chen, N.H.,Counago, R.M.,Djoko, K.Y.,Jennings, M.P.,Apicella, M.A.,Kobe, B.,McEwan, A.G.
A glutathione-dependent detoxification system is required for formaldehyde resistance and optimal survival of Neisseria meningitidis in biofilms.
Antioxid. Redox Signal., 18:743-755, 2013

PubMed Abstract: The glutathione-dependent AdhC-EstD formaldehyde detoxification system is found in eukaryotes and prokaryotes. It is established that it confers protection against formaldehyde that is produced from environmental sources or methanol metabolism. Thus, its presence in the human host-adapted bacterial pathogen Neisseria meningitidis is intriguing. This work defined the biological function of this system in the meningococcus using phenotypic analyses of mutants linked to biochemical and structural characterization of purified enzymes.

PubMed: 22937752
DOI: 10.1089/ars.2012.4749

Experimental method

X-RAY DIFFRACTION (1.4 Å)