Structure of WbdD : a bifunctional kinase and methyltransferase that regulates the chain length of the O antigen in E scherichia coli O9a-Reference-Cited by-同舟云学术

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Structure of WbdD : a bifunctional kinase and methyltransferase that regulates the chain length of the O antigen in E scherichia coli O9a

Published:2012-09-27 Issue:3 Volume:86 Page:730-742
ISSN:0950-382X
Container-title:Molecular Microbiology
language:en
Short-container-title:Molecular Microbiology

Author:

Hagelueken Gregor¹,Huang Hexian¹,Clarke Bradley R.²,Lebl Tomas³,Whitfield Chris²,Naismith James H.¹

Affiliation:

1. Biomedical Sciences Research Complex University of St Andrews North Haugh St Andrews Fife KY16 9ST UK

2. Department of Molecular and Cellular Biology University of Guelph Guelph Ontario N1G 2W1 Canada

3. School of Chemistry University of St Andrews North Haugh St Andrews Fife KY16 9ST UK

Funder

Wellcome Trust Program

Canadian Institutes of Health Research

Publisher

Wiley

Subject

Molecular Biology,Microbiology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1111/mmi.12014

Reference45 articles.

1. PHENIX: building new software for automated crystallographic structure determination

2. Crystal Structures of NodS N-Methyltransferase from Bradyrhizobium japonicum in Ligand-Free Form and as SAH Complex

3. Activation Mechanism of the MAP Kinase ERK2 by Dual Phosphorylation

4. MolProbity: all-atom structure validation for macromolecular crystallography

5. Nonreducing Terminal Modifications Determine the Chain Length of Polymannose O Antigens of Escherichia coli and Couple Chain Termination to Polymer Export via an ATP-binding Cassette Transporter

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