2pee
From Proteopedia
|
Crystal Structure of a Thermophilic Serpin, Tengpin, in the Native State
Overview
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.
About this Structure
2PEE is a Single protein structure of sequence from Thermoanaerobacter tengcongensis with and as ligands. Full crystallographic information is available from OCA.
Reference
The N terminus of the serpin, tengpin, functions to trap the metastable native state., Zhang Q, Buckle AM, Law RH, Pearce MC, Cabrita LD, Lloyd GJ, Irving JA, Smith AI, Ruzyla K, Rossjohn J, Bottomley SP, Whisstock JC, EMBO Rep. 2007 Jun 8;. PMID:17557112
Page seeded by OCA on Wed Jan 23 14:29:28 2008
