3RNZ

Crystal structure of Bacillus Amyloliquefaciens Pyroglutamyl Peptidase I

Summary for 3RNZ

• Entry DOI: 10.2210/pdb3rnz/pdb
• Related: 3RO0 3RO1
• Descriptor: Pyrrolidone-carboxylate peptidase (2 entities in total)
• Functional Keywords: hydrolase
• Biological source: Bacillus amyloliquefaciens
• Total number of polymer chains: 4
• Total formula weight: 97506.76

Authors

Lo, Y.-C.,Wang, A.H.-J. (deposition date: 2011-04-24, release date: 2011-10-05, Last modification date: 2023-11-01)

Primary citation

Lo, Y.-C.,Su, W.-C.,Ko, T.-P.,Wang, N.-C.,Wang, A.H.-J.
Terpyridine platinum(II) complexes inhibit cysteine proteases by binding to active-site cysteine.
J.Biomol.Struct.Dyn., 29:267-282, 2011

PubMed Abstract: Platinum(II) complexes have been demonstrated to form covalent bonds with sulfur-donating ligands (in glutathione, metallothionein and other sulfur-containing biomolecules) or coordination bonds with nitrogen-donating ligands (such as histidine and guanine). To investigate how these compounds interact with cysteine proteases, we chose terpyridine platinum(II) (TP-Pt(II)) complexes as a model system. By using X-ray crystallography, we demonstrated that TP-Pt(II) formed a covalent bond with the catalytic cysteine residue in pyroglutamyl peptidase I. Moreover, by using MALDI (matrix-assisted laser desorption/ionization) and TOF-TOF (time of flight) mass spectrometry, we elucidated that the TP-Pt(II) complex formed a covalent bond with the active-site cysteine residue in two other types of cysteine protease. Taken together, the results unequivocally showed that TP-Pt(II) complexes can selectively bind to the active site of most cysteine proteases. Our findings here can be useful in the design of new anti-cancer, anti-parasite or anti-virus platinum(II) compounds.

PubMed: 21875148
DOI: 10.1080/073911011010524993

Experimental method

X-RAY DIFFRACTION (2.01 Å)