6TKU
Crystal structure of a capsule-specific depolymerase produced by Klebsiella phage
Summary for 6TKU
| Entry DOI | 10.2210/pdb6tku/pdb |
| Descriptor | depolymerase KP32gp38 (2 entities in total) |
| Functional Keywords | klebsiella pneumoniae capsule, phage depolymerase, tail fiber branching system, hydrolase |
| Biological source | Klebsiella phage KP32 |
| Total number of polymer chains | 1 |
| Total formula weight | 63317.25 |
| Authors | Berisio, R.,Squeglia, F. (deposition date: 2019-11-29, release date: 2020-04-22, Last modification date: 2024-10-16) |
| Primary citation | Squeglia, F.,Maciejewska, B.,Latka, A.,Ruggiero, A.,Briers, Y.,Drulis-Kawa, Z.,Berisio, R. Structural and Functional Studies of a Klebsiella Phage Capsule Depolymerase Tailspike: Mechanistic Insights into Capsular Degradation. Structure, 28:613-, 2020 Cited by PubMed Abstract: Capsule polysaccharide is a major virulence factor of Klebsiella pneumoniae, a nosocomial pathogen associated with a wide range of infections. It protects bacteria from harsh environmental conditions, immune system response, and phage infection. To access cell wall-located receptors, some phages possess tailspike depolymerases that degrade the capsular polysaccharide. Here, we present the crystal structure of a tailspike against Klebsiella, KP32gp38, whose primary sequence shares no similarity to other proteins of known structure. In the trimeric structure of KP32gp38, each chain contains a flexible N-terminal domain, a right-handed parallel β helix domain and two β sandwiches with carbohydrate binding features. The crystal structure and activity assays allowed us to locate the catalytic site. Also, our data provide experimental evidence of a branching architecture of depolymerases in KP32 Klebsiella viruses, as KP32gp38 displays nanomolar affinity to another depolymerase from the same phage, KP32gp37. Results provide a structural framework for enzyme engineering to produce serotype-broad-active enzyme complexes against K. pneumoniae. PubMed: 32386574DOI: 10.1016/j.str.2020.04.015 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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