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3RO0

Crystal structure of Bacillus amyloliquefaciens pyroglutamyl peptidase I and terpyridine platinum(II)

Summary for 3RO0
Entry DOI10.2210/pdb3ro0/pdb
Related3RNZ 3RO1
DescriptorPyrrolidone-carboxylate peptidase, 2,2':6',2''-TERPYRIDINE PLATINUM(II) Chloride (3 entities in total)
Functional Keywordshydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
Biological sourceBacillus amyloliquefaciens
Total number of polymer chains4
Total formula weight99825.75
Authors
Lo, Y.-C.,Wang, A.H.-J. (deposition date: 2011-04-25, release date: 2011-10-05, Last modification date: 2023-11-01)
Primary citationLo, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.5 Å)
Structure validation

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