7TPU
Crystal structure of a chitinase-modifying protein from Fusarium vanettenii (Fvan-cmp)
Summary for 7TPU
| Entry DOI | 10.2210/pdb7tpu/pdb |
| Descriptor | Beta-lactamase domain-containing protein, alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
| Functional Keywords | polyglycine hydrolase, chitinase-modifying protein, serine protease, beta lactamase-like, hydrolase |
| Biological source | Fusarium vanettenii |
| Total number of polymer chains | 1 |
| Total formula weight | 69586.82 |
| Authors | Dowling, N.V.,Naumann, T.A.,Price, N.P.J.,Rose, D.R. (deposition date: 2022-01-26, release date: 2023-02-15, Last modification date: 2024-11-06) |
| Primary citation | Dowling, N.V.,Naumann, T.A.,Price, N.P.J.,Rose, D.R. Crystal structure of a polyglycine hydrolase determined using a RoseTTAFold model. Acta Crystallogr D Struct Biol, 79:168-176, 2023 Cited by PubMed Abstract: Polyglycine hydrolases (PGHs) are secreted fungal proteases that cleave the polyglycine linker of Zea mays ChitA, a defensive chitinase, thus overcoming one mechanism of plant resistance to infection. Despite their importance in agriculture, there has been no previous structural characterization of this family of proteases. The objective of this research was to investigate the proteolytic mechanism and other characteristics by structural and biochemical means. Here, the first atomic structure of a polyglycine hydrolase was identified. It was solved by X-ray crystallography using a RoseTTAFold model, taking advantage of recent technical advances in structure prediction. PGHs are composed of two domains: the N- and C-domains. The N-domain is a novel tertiary fold with an as-yet unknown function that is found across all kingdoms of life. The C-domain shares structural similarities with class C β-lactamases, including a common catalytic nucleophilic serine. In addition to insights into the PGH family and its relationship to β-lactamases, the results demonstrate the power of complementing experimental structure determination with new computational techniques. PubMed: 36762862DOI: 10.1107/S2059798323000311 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.194 Å) |
Structure validation
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