Specificity of Campylobacter jejuni Adhesin PEB3 for Phosphates and Structural Differences among Its Ligand Complexes,-Reference-Cited by-同舟云学术

Specificity of Campylobacter jejuni Adhesin PEB3 for Phosphates and Structural Differences among Its Ligand Complexes,

Published:2009-03-20 Issue:14 Volume:48 Page:3057-3067
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Min Tongpil¹,Vedadi Masoud¹,Watson David C.¹,Wasney Gregory A.¹,Munger Christine¹,Cygler Miroslaw¹,Matte Allan¹,Young N. Martin¹

Affiliation:

1. Department of Biochemistry, McGill University, Montreal, QC, H3G 1Y6 Canada, Structural Genomics Consortium, University of Toronto, and Institute for Biological Sciences, National Research Council of Canada, Ottawa, ON, K1A 0R6 Canada, and Biotechnology Research Institute, National Research Council of Canada, Montreal, QC, H4P 2R2 Canada

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi802195d

Reference37 articles.

1. Structure of the N-Linked Glycan Present on Multiple Glycoproteins in the Gram-negative Bacterium, Campylobacter jejuni

2. Definition of the bacterial N-glycosylation site consensus sequence

3. Structural context for proteinN-glycosylation in bacteria: The structure of PEB3, an adhesin fromCampylobacter jejuni

4. The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences

5. The Campylobacter jejuni PEB1a adhesin is an aspartate/glutamate-binding protein of an ABC transporter essential for microaerobic growth on dicarboxylic amino acids

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