6ZTK
Crystal structure of Mialostatin, a gut cystatin from the hard tick Ixodes ricinus
Summary for 6ZTK
| Entry DOI | 10.2210/pdb6ztk/pdb |
| Descriptor | Mialostatin, FRAGMENT OF TRITON X-100, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | cystatin, protease inhibitor, ixodes ricinus, tick, hydrolase inhibitor, protein binding |
| Biological source | Ixodes ricinus (Common tick) |
| Total number of polymer chains | 2 |
| Total formula weight | 32531.17 |
| Authors | Busa, M.,Rezacova, P.,Mares, M. (deposition date: 2020-07-20, release date: 2021-06-02, Last modification date: 2024-10-23) |
| Primary citation | Kotal, J.,Busa, M.,Urbanova, V.,Rezacova, P.,Chmelar, J.,Langhansova, H.,Sojka, D.,Mares, M.,Kotsyfakis, M. Mialostatin, a Novel Midgut Cystatin from Ixodes ricinus Ticks: Crystal Structure and Regulation of Host Blood Digestion. Int J Mol Sci, 22:-, 2021 Cited by PubMed Abstract: The hard tick is a vector of Lyme disease and tick-borne encephalitis. Host blood protein digestion, essential for tick development and reproduction, occurs in tick midgut digestive cells driven by cathepsin proteases. Little is known about the regulation of the digestive proteolytic machinery of . Here we characterize a novel cystatin-type protease inhibitor, mialostatin, from the midgut. Blood feeding rapidly induced mialostatin expression in the gut, which continued after tick detachment. Recombinant mialostatin inhibited a number of digestive cysteine cathepsins, with the greatest potency observed against cathepsin L isoforms, with which it co-localized in midgut digestive cells. The crystal structure of mialostatin was determined at 1.55 Å to explain its unique inhibitory specificity. Finally, mialostatin effectively blocked in vitro proteolysis of blood proteins by midgut cysteine cathepsins. Mialostatin is likely to be involved in the regulation of gut-associated proteolytic pathways, making midgut cystatins promising targets for tick control strategies. PubMed: 34065290DOI: 10.3390/ijms22105371 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.55 Å) |
Structure validation
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