1MTP

The X-ray crystal structure of a serpin from a thermophilic prokaryote

Summary for 1MTP

• Entry DOI: 10.2210/pdb1mtp/pdb
• Descriptor: Serine Proteinase Inhibitor (SERPIN), Chain A, Serine Proteinase Inhibitor (SERPIN), Chain B (3 entities in total)
• Functional Keywords: structural genomics, protease inhibitor
• Biological source: Thermobifida fusca; More
• Total number of polymer chains: 2
• Total formula weight: 39764.50

Authors

Irving, J.A.,Cabrita, L.D.,Rossjohn, J.,Pike, R.N.,Bottomley, S.P.,Whisstock, J.C. (deposition date: 2002-09-21, release date: 2003-04-15, Last modification date: 2024-02-14)

Primary citation

Irving, J.A.,Cabrita, L.D.,Rossjohn, J.,Pike, R.N.,Bottomley, S.P.,Whisstock, J.C.
The 1.5 A crystal structure of a prokaryote serpin: controlling conformational change in a heated environment
Structure, 11:387-397, 2003

PubMed Abstract: Serpins utilize conformational change to inhibit target proteinases; the price paid for this conformational flexibility is that many undergo temperature-induced polymerization. Despite this thermolability, serpins are present in the genomes of thermophilic prokaryotes, and here we characterize the first such serpin, thermopin. Thermopin is a proteinase inhibitor and, in comparison with human alpha(1)-antitrypsin, possesses enhanced stability at 60 degrees C. The 1.5 A crystal structure reveals novel structural features in regions implicated in serpin folding and stability. Thermopin possesses a C-terminal "tail" that interacts with the top of the A beta sheet and plays an important role in the folding/unfolding of the molecule. These data provide evidence as to how this unusual serpin has adapted to fold and function in a heated environment.

PubMed: 12679017
DOI: 10.1016/S0969-2126(03)00057-1

Experimental method

X-RAY DIFFRACTION (1.5 Å)