Structure of WbdD: A Bifunctional Kinase and Methyltransferase That Regulates the Chain Length of the O Antigen inEscherichia coliO9a

Molecular Microbiology- United Kingdom

doi 10.1111/mmi.12014

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September 27, 2012

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Wiley

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Structure of WbdD: A Bifunctional Kinase and Methyltransferase That Regulates the Chain Length of the O Antigen inEscherichia coliO9a

Molecular Microbiology- United Kingdom

Full Text

Abstract

Categories

Date

Authors

Publisher

Related search

Biochemical and Structural Analysis of Bacterial O-Antigen Chain Length Regulator Proteins Reveals a Conserved Quaternary Structure

Structural Characterization of Closely Related O-Antigen Lipopolysaccharide (LPS) Chain Length Regulators

A CDK-related Kinase Regulates the Length and Assembly of Flagella inChlamydomonas

Syk Is a Dual-Specificity Kinase That Self-Regulates the Signal Output From the B-Cell Antigen Receptor

Mutagenesis and Chemical Cross-Linking Suggest That WZZ Dimer Stability and Oligomerization Affect Lipopolysaccharide O-Antigen Modal Chain Length Control

Crystal Structures of the Bifunctional tRNA Methyltransferase Trm5a

Structure and Mechanism of the Rebeccamycin Sugar 4′-O-Methyltransferase RebM

the Structure and Catalytic Mechanism of Sorghum Bicolor Caffeoyl-CoA O -Methyltransferase

Unique Regions of the Polysaccharide Co-Polymerase Wzz2 From Pseudomonas Aeruginosa Are Essential for O-Specific Antigen Chain Length Control