4RWR
2.1 Angstrom Crystal Structure of Stage II Sporulation Protein D from Bacillus anthracis
Summary for 4RWR
| Entry DOI | 10.2210/pdb4rwr/pdb |
| Descriptor | Stage II sporulation protein D (2 entities in total) |
| Functional Keywords | structural genomics, niaid, national institute of allergy and infectious diseases, center for structural genomics of infectious diseases, csgid, stage ii sporulation protein d, spoiid, germination, viral protein |
| Biological source | Bacillus anthracis (anthrax,anthrax bacterium) |
| Total number of polymer chains | 2 |
| Total formula weight | 74110.90 |
| Authors | Minasov, G.,Wawrzak, Z.,Nocadello, S.,Shuvalova, L.,Dubrovska, I.,Flores, K.,Bagnoli, F.,Falugi, F.,Bottomley, M.,Grandi, G.,Anderson, W.F.,Center for Structural Genomics of Infectious Diseases (CSGID) (deposition date: 2014-12-05, release date: 2014-12-17, Last modification date: 2024-11-06) |
| Primary citation | Nocadello, S.,Minasov, G.,Shuvalova, L.S.,Dubrovska, I.,Sabini, E.,Anderson, W.F. Crystal Structures of the SpoIID Lytic Transglycosylases Essential for Bacterial Sporulation. J.Biol.Chem., 291:14915-14926, 2016 Cited by PubMed Abstract: Bacterial spores are the most resistant form of life known on 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. Stage II sporulation protein D (SpoIID) is a lytic transglycosylase (LT) essential for sporulation. The LT superfamily is a potential drug target because it is active in essential bacterial processes involving the peptidoglycan, 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. PubMed: 27226615DOI: 10.1074/jbc.M116.729749 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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