Structural highlights
5i1t is a 1 chain structure with sequence from Clostridioides difficile 630. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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Method: | X-ray diffraction, Resolution 2.6Å |
Ligands: | , , , , , |
Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
Q18CL6_CLOD6
Publication Abstract from PubMed
Bacterial spores are the most resistant form of life known on the Earth and represent a serious problem for i) bioterrorism attack, ii) horizontal transmission of microbial pathogens in the community and iii) persistence in patients and in a nosocomial environment. SpoIID (Stage II Sporulation Protein D) is a Lytic Transglycosylase (LT) essential for sporulation. The LT-superfamily is a potential drug target because they are active in essential bacterial processes involving the peptidoglycan (PGN), which is unique to bacteria. However, the absence of structural information for the sporulation specific LT enzymes has hindered mechanistic understanding of SpoIID. Here, we report the first crystal structures with and without ligands of the SpoIID family from two community relevant spore-forming pathogens, Bacillus anthracis and Clostridium difficile. The structures allow us to visualize the overall architecture, characterize the substrate recognition model, identify critical residues and provide the structural basis for catalysis by this new family of enzymes.
Crystal structures of the SpoIID lytic transglycosylases essential for bacterial sporulation.,Nocadello S, Minasov G, Shuvalova LS, Dubrovska I, Sabini E, Anderson WF J Biol Chem. 2016 May 18. pii: jbc.M116.729749. PMID:27226615[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Nocadello S, Minasov G, Shuvalova LS, Dubrovska I, Sabini E, Anderson WF. Crystal structures of the SpoIID lytic transglycosylases essential for bacterial sporulation. J Biol Chem. 2016 May 18. pii: jbc.M116.729749. PMID:27226615 doi:http://dx.doi.org/10.1074/jbc.M116.729749