2PEF

Crystal Structure of a Thermophilic Serpin, Tengpin, in the Latent State

Summary for 2PEF

• Entry DOI: 10.2210/pdb2pef/pdb
• Related: 2PEE
• Descriptor: Serine protease inhibitor (2 entities in total)
• Functional Keywords: serpin, protease inhibitor
• Biological source: Thermoanaerobacter tengcongensis
• Total number of polymer chains: 1
• Total formula weight: 42246.03

Authors

Zhang, Q.W.,Buckle, A.M.,Whisstock, J.C. (deposition date: 2007-04-03, release date: 2007-06-19, Last modification date: 2023-08-30)

Primary citation

Zhang, Q.,Buckle, A.M.,Law, R.H.,Pearce, M.C.,Cabrita, L.D.,Lloyd, G.J.,Irving, J.A.,Smith, A.I.,Ruzyla, K.,Rossjohn, J.,Bottomley, S.P.,Whisstock, J.C.
The N terminus of the serpin, tengpin, functions to trap the metastable native state.
Embo Rep., 8:658-663, 2007

PubMed Abstract: Serpins fold to a metastable native state and are susceptible to undergoing spontaneous conformational change to more stable conformers, such as the latent form. We investigated conformational change in tengpin, an unusual prokaryotic serpin from the extremophile Thermoanaerobacter tengcongensis. In addition to the serpin domain, tengpin contains a functionally uncharacterized 56-amino-acid amino-terminal region. Deletion of this domain creates a variant--tengpinDelta51--which folds past the native state and readily adopts the latent conformation. Analysis of crystal structures together with mutagenesis studies show that the N terminus of tengpin protects a hydrophobic patch in the serpin domain and functions to trap tengpin in its native metastable state. A 13-amino-acid peptide derived from the N terminus is able to mimick the role of the N terminus in stabilizing the native state of tengpinDelta51. Therefore, the function of the N terminus in tengpin resembles protein cofactors that prevent mammalian serpins from spontaneously adopting the latent conformation.

PubMed: 17557112
DOI: 10.1038/sj.embor.7400986

Experimental method

X-RAY DIFFRACTION (1.6 Å)