3ISY
Crystal structure of an intracellular proteinase inhibitor (ipi, bsu11130) from bacillus subtilis at 2.61 A resolution
Summary for 3ISY
| Entry DOI | 10.2210/pdb3isy/pdb |
| Descriptor | Intracellular proteinase inhibitor, TETRAETHYLENE GLYCOL (3 entities in total) |
| Functional Keywords | intracellular proteinase inhibitor bsupi, beta sandwich, greek key, structural genomics, joint center for structural genomics, jcsg, protein structure initiative, psi-2, protein binding |
| Biological source | Bacillus subtilis |
| Total number of polymer chains | 1 |
| Total formula weight | 14481.66 |
| Authors | Joint Center for Structural Genomics (JCSG) (deposition date: 2009-08-27, release date: 2009-09-15, Last modification date: 2024-10-16) |
| Primary citation | Rigden, D.J.,Xu, Q.,Chang, Y.,Eberhardt, R.Y.,Finn, R.D.,Rawlings, N.D. The first structure in a family of peptidase inhibitors reveals an unusual Ig-like fold. F1000Res, 2:154-154, 2013 Cited by PubMed Abstract: We report the crystal structure solution of the Intracellular Protease Inhibitor (IPI) protein from Bacillus subtilis, which has been reported to be an inhibitor of the intracellular subtilisin Isp1 from the same organism. The structure of IPI is a variant of the all-beta, immunoglobulin (Ig) fold. It is possible that IPI is important for protein-protein interactions, of which inhibition of Isp1 is one. The intracellular nature of ISP is questioned, because an alternative ATG codon in the ipi gene would produce a protein with an N-terminal extension containing a signal peptide. It is possible that alternative initiation exists, producing either an intracellular inhibitor or a secreted form that may be associated with the cell surface. Homologues of the IPI protein from other species are multi-domain proteins, containing signal peptides and domains also associated with the bacterial cell-surface. The cysteine peptidase inhibitors chagasin and amoebiasin also have Ig-like folds, but their topology differs significantly from that of IPI, and they share no recent common ancestor. A model of IPI docked to Isp1 shows similarities to other subtilisin:inhibitor complexes, particularly where the inhibitor interacts with the peptidase active site. PubMed: 24555072DOI: 10.12688/f1000research.2-154.v2 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.61 Å) |
Structure validation
Download full validation report
