3I6S
Crystal Structure of the plant subtilisin-like protease SBT3
Summary for 3I6S
| Entry DOI | 10.2210/pdb3i6s/pdb |
| Descriptor | Subtilisin-like protease, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-L-fucopyranose-(1-3)-[2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total) |
| Functional Keywords | subtilisin-like, protease, pa-domain, fn3-domain, hydrolase |
| Biological source | Solanum lycopersicum (tomato) |
| Total number of polymer chains | 2 |
| Total formula weight | 142368.92 |
| Authors | Rose, R.,Ottmann, C. (deposition date: 2009-07-07, release date: 2010-01-19, Last modification date: 2024-10-30) |
| Primary citation | Ottmann, C.,Rose, R.,Huttenlocher, F.,Cedzich, A.,Hauske, P.,Kaiser, M.,Huber, R.,Schaller, A. Structural basis for Ca2+-independence and activation by homodimerization of tomato subtilase 3. Proc.Natl.Acad.Sci.USA, 106:17223-17228, 2009 Cited by PubMed Abstract: Subtilases are serine proteases found in Archae, Bacteria, yeasts, and higher eukaryotes. Plants possess many more of these subtilisin-like endopeptidases than animals, e.g., 56 identified genes in Arabidopsis compared with only 9 in humans, indicating important roles for subtilases in plant biology. We report the first structure of a plant subtilase, SBT3 from tomato, in the active apo form and complexed with a chloromethylketone (cmk) inhibitor. The domain architecture comprises an N-terminal protease domain displaying a 132 aa protease-associated (PA) domain insertion and a C-terminal seven-stranded jelly-roll fibronectin (Fn) III-like domain. We present the first structural evidence for an explicit function of PA domains in proteases revealing a vital role in the homo-dimerization of SBT3 and in enzyme activation. Although Ca(2+)-binding sites are conserved and critical for stability in other subtilases, SBT3 was found to be Ca(2+)-free and its thermo stability is Ca(2+)-independent. PubMed: 19805099DOI: 10.1073/pnas.0907587106 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
Download full validation report
