1MTZ
Crystal Structure of the Tricorn Interacting Factor F1
Summary for 1MTZ
| Entry DOI | 10.2210/pdb1mtz/pdb |
| Related | 1MT3 1MU0 |
| Descriptor | Proline iminopeptidase (2 entities in total) |
| Functional Keywords | alpha-beta hydrolase, cap domain, caged active site, prolyl peptidase, hydrolase |
| Biological source | Thermoplasma acidophilum |
| Total number of polymer chains | 1 |
| Total formula weight | 33530.09 |
| Authors | Goettig, P.,Groll, M.,Kim, J.-S.,Huber, R.,Brandstetter, H. (deposition date: 2002-09-23, release date: 2002-11-06, Last modification date: 2024-10-16) |
| Primary citation | Goettig, P.,Groll, M.,Kim, J.-S.,Huber, R.,Brandstetter, H. Structures of the tricorn-interacting aminopeptidase F1 with different ligands explain its catalytic mechanism Embo J., 21:5343-5352, 2002 Cited by PubMed Abstract: F1 is a 33.5 kDa serine peptidase of the alpha/beta-hydrolase family from the archaeon Thermoplasma acidophilum. Subsequent to proteasomal protein degradation, tricorn generates small peptides, which are cleaved by F1 to yield single amino acids. We have solved the crystal structure of F1 with multiwavelength anomalous dispersion (MAD) phasing at 1.8 A resolution. In addition to the conserved catalytic domain, the structure reveals a chiefly alpha-helical domain capping the catalytic triad. Thus, the active site is accessible only through a narrow opening from the protein surface. Two structures with molecules bound to the active serine, including the inhibitor phenylalanyl chloromethylketone, elucidate the N-terminal recognition of substrates and the catalytic activation switch mechanism of F1. The cap domain mainly confers the specificity for hydrophobic side chains by a novel cavity system, which, analogously to the tricorn protease, guides substrates to the buried active site and products away from it. Finally, the structure of F1 suggests a possible functional complex with tricorn that allows efficient processive degradation to free amino acids for cellular recycling. PubMed: 12374735DOI: 10.1093/emboj/cdf552 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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