ArticleBioscience reports2013
Crystal structure of the capsular polysaccharide synthesizing protein CapE of Staphylococcus aureus.
Article in Bioscience reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 17 citations in OpenAlex.
- SDR7-6, a short-chain alcohol dehydrogenase/reductase family protein, regulates light-dependent cell death and defence responses in rice.Molecular plant pathology · 2022Article
- ThemBio · 2020Article
- Biochemical analysis of a sugar 4,6-dehydratase from Acanthamoeba polyphaga Mimivirus.Protein science : a publication of the Protein Society · 2020Article
- Genome Report-A Genome Sequence Analysis of the RB51 Strain ofG3 (Bethesda, Md.) · 2020Article
- Coordination of capsule assembly and cell wall biosynthesis in Staphylococcus aureus.Nature communications · 2019Article
- Crystal structure of a UDP-GlcNAc epimerase for surface polysaccharide biosynthesis in Acinetobacter baumannii.PloS one · 2018Article
- Structural and Biochemical Investigation of PglF from Campylobacter jejuni Reveals a New Mechanism for a Member of the Short Chain Dehydrogenase/Reductase Superfamily.Biochemistry · 2017Article
- Discovery and characterization of natural tropolones as inhibitors of the antibacterial target CapF from Staphylococcus aureus.Scientific reports · 2015Article
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- Giant virus Megavirus chilensis encodes the biosynthetic pathway for uncommon acetamido sugars.The Journal of biological chemistry · 2014Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Enzymes synthesizing the bacterial CP (capsular polysaccharide) are attractive antimicrobial targets. However, we lack critical information about the structure and mechanism of many of them. In an effort to reduce that gap, we have determined three different crystal structures of the enzyme CapE of the human pathogen Staphylococcus aureus. The structure reveals that CapE is a member of the SDR (short-chain dehydrogenase/reductase) super-family of proteins. CapE assembles in a hexameric complex stabilized by three major contact surfaces between protein subunits. Turnover of substrate and/or coenzyme induces major conformational changes at the contact interface between protein subunits, and a displacement of the substrate-binding domain with respect to the Rossmann domain. A novel dynamic element that we called the latch is essential for remodelling of the protein-protein interface. Structural and primary sequence alignment identifies a group of SDR proteins involved in polysaccharide synthesis that share the two salient features of CapE: the mobile loop (latch) and a distinctive catalytic site (MxxxK). The relevance of these structural elements was evaluated by site-directed mutagenesis.
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