3ISY

Crystal structure of an intracellular proteinase inhibitor (ipi, bsu11130) from bacillus subtilis at 2.61 A resolution

3ISY の概要

• エントリーDOI: 10.2210/pdb3isy/pdb
• 分子名称: Intracellular proteinase inhibitor, TETRAETHYLENE GLYCOL (3 entities in total)
• 機能のキーワード: intracellular proteinase inhibitor bsupi, beta sandwich, greek key, structural genomics, joint center for structural genomics, jcsg, protein structure initiative, psi-2, protein binding
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14481.66

構造登録者

Joint Center for Structural Genomics (JCSG) (登録日: 2009-08-27, 公開日: 2009-09-15, 最終更新日: 2024-10-16)

主引用文献

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

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: 24555072
DOI: 10.12688/f1000research.2-154.v2

実験手法

X-RAY DIFFRACTION (2.61 Å)