Lipopolysaccharide is an essential component of the outer membrane of Gram-negative bacteria and consists of three elements: lipid A, the core oligosaccharide and the O-antigen. The inner core region is highly conserved and contains at least one residue of 3-deoxy-d-manno-octulosonate (Kdo). The first committed step of Kdo biosynthesis is the aldol-keto isomerisation of d-ribulose 5-phosphate to d-arabinose 5-phosphate catalyzed by arabinose 5-phosphate isomerase encoded in Escherichia coli by the kdsD gene. KdsD contains an N-terminal sugar isomerase (SIS) domain commonly found in phosphosugar isomerases but its three-dimensional structure is unknown. The structure of the KdsD SIS domain has been predicted by homology modeling using the hypothetical 3etn protein as a template. Moreover by sequence alignments, comparison with other sugar isomerases structurally related to KdsD, and site-directed mutagenesis we implicated four residues in KdsD activity or substrate recognition. A possible role of these residues in the catalysis is discussed. © 2009 Elsevier Inc. All rights reserved.

Sommaruga, S., DE GIOIA, L., Tortora, P., Polissi, A. (2009). Structure prediction and functional analysis of KdsD, an enzyme involved in lipopolysaccharide biosynthesis. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 16(388), 222-227 [10.1016/j.bbrc.2009.07.154].

Structure prediction and functional analysis of KdsD, an enzyme involved in lipopolysaccharide biosynthesis

DE GIOIA, LUCA;TORTORA, PAOLO;POLISSI, ALESSANDRA
2009

Abstract

Lipopolysaccharide is an essential component of the outer membrane of Gram-negative bacteria and consists of three elements: lipid A, the core oligosaccharide and the O-antigen. The inner core region is highly conserved and contains at least one residue of 3-deoxy-d-manno-octulosonate (Kdo). The first committed step of Kdo biosynthesis is the aldol-keto isomerisation of d-ribulose 5-phosphate to d-arabinose 5-phosphate catalyzed by arabinose 5-phosphate isomerase encoded in Escherichia coli by the kdsD gene. KdsD contains an N-terminal sugar isomerase (SIS) domain commonly found in phosphosugar isomerases but its three-dimensional structure is unknown. The structure of the KdsD SIS domain has been predicted by homology modeling using the hypothetical 3etn protein as a template. Moreover by sequence alignments, comparison with other sugar isomerases structurally related to KdsD, and site-directed mutagenesis we implicated four residues in KdsD activity or substrate recognition. A possible role of these residues in the catalysis is discussed. © 2009 Elsevier Inc. All rights reserved.
Articolo in rivista - Articolo scientifico
protein chemistry
English
222
227
Sommaruga, S., DE GIOIA, L., Tortora, P., Polissi, A. (2009). Structure prediction and functional analysis of KdsD, an enzyme involved in lipopolysaccharide biosynthesis. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 16(388), 222-227 [10.1016/j.bbrc.2009.07.154].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10281/10253
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