Crystal structure analysis of the polysialic acid specific O-acetyltransferase NeuO.
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 vir...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2011-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC3046976?pdf=render |
| _version_ | 1811266255379759104 |
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| author | Eike C Schulz Anne K Bergfeld Ralf Ficner Martina Mühlenhoff |
| author_facet | Eike C Schulz Anne K Bergfeld Ralf Ficner Martina Mühlenhoff |
| author_sort | Eike C Schulz |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-04-12T20:39:53Z |
| format | Article |
| id | doaj.art-e020ea4bd81040f0bc222f42cc34bdb0 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-04-12T20:39:53Z |
| publishDate | 2011-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-e020ea4bd81040f0bc222f42cc34bdb02022-12-22T03:17:28ZengPublic Library of Science (PLoS)PLoS ONE1932-62032011-01-0163e1740310.1371/journal.pone.0017403Crystal structure analysis of the polysialic acid specific O-acetyltransferase NeuO.Eike C SchulzAnne K BergfeldRalf FicnerMartina MühlenhoffThe 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.http://europepmc.org/articles/PMC3046976?pdf=render |
| spellingShingle | Eike C Schulz Anne K Bergfeld Ralf Ficner Martina Mühlenhoff Crystal structure analysis of the polysialic acid specific O-acetyltransferase NeuO. PLoS ONE |
| title | Crystal structure analysis of the polysialic acid specific O-acetyltransferase NeuO. |
| title_full | Crystal structure analysis of the polysialic acid specific O-acetyltransferase NeuO. |
| title_fullStr | Crystal structure analysis of the polysialic acid specific O-acetyltransferase NeuO. |
| title_full_unstemmed | Crystal structure analysis of the polysialic acid specific O-acetyltransferase NeuO. |
| title_short | Crystal structure analysis of the polysialic acid specific O-acetyltransferase NeuO. |
| title_sort | crystal structure analysis of the polysialic acid specific o acetyltransferase neuo |
| url | http://europepmc.org/articles/PMC3046976?pdf=render |
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