1os0

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Thermolysin with an alpha-amino phosphinic inhibitor

Structural highlights

1os0 is a 1 chain structure with sequence from Bacillus thermoproteolyticus. This structure supersedes the now removed PDB entry 1no0. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.1Å
Ligands:0PQ, CA, DMS, ZN
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

THER_BACTH Extracellular zinc metalloprotease.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

A new alpha-aminophosphinic compound able to inhibit both zinc-containing exopeptidases and endopeptidases has been crystallized with TLN as a model in order to investigate the mode of zinc recognition by the phosphinic moiety and to evaluate the potential role of the free alpha-amino group in the formation of enzyme-inhibitor complexes. In addition to the main interactions between the backbone of the inhibitor and the enzyme active site, it is observed that the phosphinic group acts as a distorted bidentate ligand for the zinc ion, while the free alpha-amino function does not directly participate in interactions within the active site. Association of the present data and the K(i) values of various analogues of the inhibitor towards TLN and neprilysin suggests differences in the hydrophobicity of the S(1)-S(2) domains of the enzymes. This could be taken into account in the design of selective inhibitors.

Interactions of a new alpha-aminophosphinic derivative inside the active site of TLN (thermolysin): a model for zinc-metalloendopeptidase inhibition.,Selkti M, Tomas A, Gaucher JF, Prange T, Fournie-Zaluski MC, Chen H, Roques BP Acta Crystallogr D Biol Crystallogr. 2003 Jul;59(Pt 7):1200-5. Epub 2003, Jun 27. PMID:12832763[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
1 reviews cite this structure
Phosphinic Peptides as Tool Compounds for the Study of Pharmacologically Relevant Zn-Metalloproteases.
Georgiadis et al. (2022)
0 more
5 other articles
No citations found

See Also

References

  1. ↑ Selkti M, Tomas A, Gaucher JF, Prange T, Fournie-Zaluski MC, Chen H, Roques BP. Interactions of a new alpha-aminophosphinic derivative inside the active site of TLN (thermolysin): a model for zinc-metalloendopeptidase inhibition. Acta Crystallogr D Biol Crystallogr. 2003 Jul;59(Pt 7):1200-5. Epub 2003, Jun 27. PMID:12832763

Contents


PDB ID 1os0

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OCA

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