ArticleActa crystallographica. Section D, Biological crystallography2015
Structure of Csd3 from Helicobacter pylori, a cell shape-determining metallopeptidase.
Article in Acta crystallographica. Section D, Biological crystallography, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 25 citations in OpenAlex.
- Research advances of the establishment and characterization ofFrontiers in microbiology · 2025Review
- Novel M23 peptidases Pgp4, Pgp5, and Pgp6 contribute to helical cell shape inFrontiers in microbiology · 2025Article
- Heterodimerization of staphylococcal phage φ2638A endolysin isoforms and their functional role in bacterial lysis.microLife · 2025Article
- MultipleFrontiers in microbiology · 2023Article
- One fold, many functions-M23 family of peptidoglycan hydrolases.Frontiers in microbiology · 2022Review
- Diversification of LytM Protein Functions in Polar Elongation and Cell Division ofFrontiers in microbiology · 2021Article
- Structural basis of peptidoglycan endopeptidase regulation.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Nonhelical Helicobacter pylori Mutants Show Altered Gland Colonization and Elicit Less Gastric Pathology than Helical Bacteria during Chronic Infection.Infection and immunity · 2019Article
- Morphology ofPrzeglad gastroenterologiczny · 2018Review
- 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
- The Cell Shape-determining Csd6 Protein from Helicobacter pylori Constitutes a New Family of L,D-Carboxypeptidase.The Journal of biological chemistry · 2015Article
- Pathogenesis of Helicobacter pylori Infection.Helicobacter · 2015Review
Corrections and comments
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Authors and funding
13 authors at 4 institutions in 2 countries.
Funding
Abstract
Helicobacter pylori is associated with various gastrointestinal diseases such as gastritis, ulcers and gastric cancer. Its colonization of the human gastric mucosa requires high motility, which depends on its helical cell shape. Seven cell shape-determining genes (csd1, csd2, csd3/hdpA, ccmA, csd4, csd5 and csd6) have been identified in H. pylori. Their proteins play key roles in determining the cell shape through modifications of the cell-wall peptidoglycan by the alteration of cross-linking or by the trimming of peptidoglycan muropeptides. Among them, Csd3 (also known as HdpA) is a bifunctional enzyme. Its D,D-endopeptidase activity cleaves the D-Ala(4)-mDAP(3) peptide bond between cross-linked muramyl tetrapeptides and pentapeptides. It is also a D,D-carboxypeptidase that cleaves off the terminal D-Ala(5) from the muramyl pentapeptide. Here, the crystal structure of this protein has been determined, revealing the organization of its three domains in a latent and inactive state. The N-terminal domain 1 and the core of domain 2 share the same fold despite a very low level of sequence identity, and their surface-charge distributions are different. The C-terminal LytM domain contains the catalytic site with a Zn(2+) ion, like the similar domains of other M23 metallopeptidases. Domain 1 occludes the active site of the LytM domain. The core of domain 2 is held against the LytM domain by the C-terminal tail region that protrudes from the LytM domain.
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