3JQY

Crystal Structure of the polySia specific acetyltransferase NeuO

Summary for 3JQY

• Entry DOI: 10.2210/pdb3jqy/pdb
• Descriptor: Polysialic acid O-acetyltransferase, DI(HYDROXYETHYL)ETHER, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: o-acetyltransferase, left-handed beta-helix polysia, transferase
• Biological source: Escherichia coli
• Total number of polymer chains: 3
• Total formula weight: 84802.97

Authors

Schulz, E.-C.,Bergfeld, A.,Muehlenhoff, M.,Ficner, R. (deposition date: 2009-09-08, release date: 2010-08-18, Last modification date: 2024-04-03)

Primary citation

Schulz, E.C.,Bergfeld, A.K.,Ficner, R.,Muhlenhoff, M.
Crystal structure analysis of the polysialic acid specific O-acetyltransferase NeuO
PLoS ONE, 6:e17403-e17403, 2011

PubMed Abstract: The major virulence factor of the neuroinvasive pathogen Escherichia coli K1 is the K1 capsule composed of α2,8-linked polysialic acid (polySia). K1 strains harboring the CUS-3 prophage modify their capsular polysaccharide by phase-variable O-acetylation, a step that is associated with increased virulence. Here we present the crystal structure of the prophage-encoded polysialate O-acetyltransferase NeuO. The homotrimeric enzyme belongs to the left-handed β-helix (LβH) family of acyltransferases and is characterized by an unusual funnel-shaped outline. Comparison with other members of the LβH family allowed the identification of active site residues and proposal of a catalytic mechanism and highlighted structural characteristics of polySia specific O-acetyltransferases. As a unique feature of NeuO, the enzymatic activity linearly increases with the length of the N-terminal poly-ψ-domain which is composed of a variable number of tandem copies of an RLKTQDS heptad. Since the poly-ψ-domain was not resolved in the crystal structure it is assumed to be unfolded in the apo-enzyme.

PubMed: 21390252
DOI: 10.1371/journal.pone.0017403

Experimental method

X-RAY DIFFRACTION (1.699 Å)