ArticleThe Journal of biological chemistry2015
The Cell Shape-determining Csd6 Protein from Helicobacter pylori Constitutes a New Family of L,D-Carboxypeptidase.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 35 citations in OpenAlex.
- Assembly and glycosylation ofPNAS nexus · 2026Article
- Secretome analysis and virulence assessment inJournal of oral microbiology · 2024Article
- The Silkworm Carboxypeptidase Inhibitor Prevents Gastric Cancer Cells' Proliferation through the EGF/EGFR Signaling Pathway.International journal of molecular sciences · 2023Article
- Asymmetric peptidoglycan editing generates cell curvature in Bdellovibrio predatory bacteria.Nature communications · 2022Article
- Morphological change of coiled bacterium Spirosoma linguale with acquisition of β-lactam resistance.Scientific reports · 2021Article
- Cleavage of Braun's lipoprotein Lpp from the bacterial peptidoglycan by a paralog of l,d-transpeptidases, LdtF.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Article
- Cell morphology as a virulence determinant: lessons from Helicobacter pylori.Current opinion in microbiology · 2020Review
- Nonhelical Helicobacter pylori Mutants Show Altered Gland Colonization and Elicit Less Gastric Pathology than Helical Bacteria during Chronic Infection.Infection and immunity · 2019Article
- Potential Role of Biofilm Formation in the Development of Digestive Tract Cancer With Special Reference toFrontiers in microbiology · 2019Article
- Cell Wall Hydrolases in Bacteria: Insight on the Diversity of Cell Wall Amidases, Glycosidases and Peptidases Toward Peptidoglycan.Frontiers in microbiology · 2019Review
- Morphology ofPrzeglad gastroenterologiczny · 2018Review
- Article
- Determinants of Bacterial Morphology: From Fundamentals to Possibilities for Antimicrobial Targeting.Frontiers in microbiology · 2017Review
- The Helical Shape of Campylobacter jejuni Promotes In Vivo Pathogenesis by Aiding Transit through Intestinal Mucus and Colonization of Crypts.Infection and immunity · 2016Article
- Structural Basis of the Heterodimer Formation between Cell Shape-Determining Proteins Csd1 and Csd2 from Helicobacter pylori.PloS one · 2016Article
- Isolation, Purification and Characterization of L,D-transpeptidase 2 from Mycobacterium tuberculosis.Acta naturaeArticle
- Peptidoglycan binding by a pocket on the accessory NTF2-domain of Pgp2 directs helical cell shape of Campylobacter jejuni.The Journal of biological chemistryArticle
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Authors and funding
20 authors at 7 institutions in 2 countries.
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Abstract
Helicobacter pylori causes gastrointestinal diseases, including gastric cancer. Its high motility in the viscous gastric mucosa facilitates colonization of the human stomach and depends on the helical cell shape and the flagella. In H. pylori, Csd6 is one of the cell shape-determining proteins that play key roles in alteration of cross-linking or by trimming of peptidoglycan muropeptides. Csd6 is also involved in deglycosylation of the flagellar protein FlaA. To better understand its function, biochemical, biophysical, and structural characterizations were carried out. We show that Csd6 has a three-domain architecture and exists as a dimer in solution. The N-terminal domain plays a key role in dimerization. The middle catalytic domain resembles those of l,d-transpeptidases, but its pocket-shaped active site is uniquely defined by the four loops I to IV, among which loops I and III show the most distinct variations from the known l,d-transpeptidases. Mass analyses confirm that Csd6 functions only as an l,d-carboxypeptidase and not as an l,d-transpeptidase. The d-Ala-complexed structure suggests possible binding modes of both the substrate and product to the catalytic domain. The C-terminal nuclear transport factor 2-like domain possesses a deep pocket for possible binding of pseudaminic acid, and in silico docking supports its role in deglycosylation of flagellin. On the basis of these findings, it is proposed that H. pylori Csd6 and its homologs constitute a new family of l,d-carboxypeptidase. This work provides insights into the function of Csd6 in regulating the helical cell shape and motility of H. pylori.
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