3UL5
Saccharum officinarum canecystatin-1 in space group C2221
Summary for 3UL5
| Entry DOI | 10.2210/pdb3ul5/pdb |
| Related | 3UL6 |
| Descriptor | Canecystatin-1, GLYCEROL, SODIUM ION, ... (4 entities in total) |
| Functional Keywords | cystatin, defense, hydrolase inhibitor |
| Biological source | Saccharum officinarum (noble cane,sugarcane) |
| Total number of polymer chains | 4 |
| Total formula weight | 61676.63 |
| Authors | Valadares, N.F.,Pereira, H.M.,Oliveira-Silva, R.,Garratt, R.C. (deposition date: 2011-11-10, release date: 2012-11-28, Last modification date: 2023-09-13) |
| Primary citation | Valadares, N.F.,de Oliveira-Silva, R.,Cavini, I.A.,Marques, I.A.,Pereira, H.D.,Soares-Costa, A.,Henrique-Silva, F.,Kalbitzer, H.R.,Munte, C.E.,Garratt, R.C. X-ray crystallography and NMR studies of domain-swapped canecystatin-1. Febs J., 280:1028-1038, 2013 Cited by PubMed Abstract: The three-dimensional structure of canecystatin-1, a potent inhibitor of cysteine proteases from sugarcane (Saccharum officinarum), has been solved in two different crystal forms. In both cases, it is seen to exist as a domain-swapped dimer, the first such observation for a cystatin of plant origin. Size exclusion chromatography and multidimensional NMR spectroscopy show the dimer to be the dominant species in solution, despite the presence of a measurable quantity of monomer undergoing slow exchange. The latter is believed to be the active species, whereas the domain-swapped dimer is presumably inactive, as its first inhibitory loop has been extended to form part of a long β-strand that forms a double-helical coiled coil with its partner from the other monomer. A similar structure is observed in human cystatin C, but the spatial disposition of the two lobes of the dimer is rather different. Dimerization is presumably a mechanism by which canecystatin-1 can be kept inactive within the plant, avoiding the inhibition of endogenous proteases. The structure described here provides a platform for the rational design of specific cysteine protease inhibitors for biotechnological applications. PubMed: 23241243DOI: 10.1111/febs.12095 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
Download full validation report
