4K40

Peptidoglycan O-acetylesterase in action, 0 min

Summary for 4K40

• Entry DOI: 10.2210/pdb4k40/pdb
• Related: 4K3U
• Descriptor: GDSL-like Lipase/Acylhydrolase family protein (2 entities in total)
• Functional Keywords: alpha/beta fold, peptidoglycan hydrolase, hydrolase
• Biological source: Neisseria meningitidis LNP21362
• Total number of polymer chains: 2
• Total formula weight: 81581.58

Authors

Williams, A.H.,Gompert Boneca, I. (deposition date: 2013-04-11, release date: 2014-09-03, Last modification date: 2024-10-30)

Primary citation

Williams, A.H.,Veyrier, F.J.,Bonis, M.,Michaud, Y.,Raynal, B.,Taha, M.K.,White, S.W.,Haouz, A.,Boneca, I.G.
Visualization of a substrate-induced productive conformation of the catalytic triad of the Neisseria meningitidis peptidoglycan O-acetylesterase reveals mechanistic conservation in SGNH esterase family members.
Acta Crystallogr.,Sect.D, 70:2631-2639, 2014

PubMed Abstract: Peptidoglycan O-acetylesterase (Ape1), which is required for host survival in Neisseria sp., belongs to the diverse SGNH hydrolase superfamily, which includes important viral and bacterial virulence factors. Here, multi-domain crystal structures of Ape1 with an SGNH catalytic domain and a newly identified putative peptidoglycan-detection module are reported. Enzyme catalysis was performed in Ape1 crystals and key catalytic intermediates along the SGNH esterase hydrolysis reaction pathway were visualized, revealing a substrate-induced productive conformation of the catalytic triad, a mechanistic detail that has not previously been observed. This substrate-induced productive conformation of the catalytic triad shifts the established dogma on these enzymes, generating valuable insight into the structure-based design of drugs targeting the SGNH esterase superfamily.

PubMed: 25286847
DOI: 10.1107/S1399004714016770

Experimental method

X-RAY DIFFRACTION (2.634 Å)