1zfl
From Proteopedia
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Solution structure of III-A, the major intermediate in the oxidative folding of leech carboxypeptidase inhibitor
Overview
The III-A intermediate constitutes the major rate-determining step in the, oxidative folding of leech carboxypeptidase inhibitor (LCI). In this work, III-A has been directly purified from the folding reaction and, structurally characterized by NMR spectroscopy. This species, containing, three native disulfides, displays a highly native-like structure; however, it lacks some secondary structure elements, making it more flexible than, native LCI. III-A represents a structurally determined example of a, disulfide-insecure intermediate; direct oxidation of this species to the, fully native protein seems to be restricted by the burial of its two free, cysteine residues inside a native-like structure. We also show that, theoretical approaches based on topological constraints predict with good, accuracy the presence of this folding intermediate. Overall, the derived, results suggest that, as it occurs with non-disulfide bonded proteins, native-like interactions between segments of secondary structure rather, than the crosslinking of disulfide bonds direct the folding of LCI.
About this Structure
1ZFL is a Single protein structure of sequence from Hirudo medicinalis. Full crystallographic information is available from OCA.
Reference
NMR structural characterization and computational predictions of the major intermediate in oxidative folding of leech carboxypeptidase inhibitor., Arolas JL, D'Silva L, Popowicz GM, Aviles FX, Holak TA, Ventura S, Structure. 2005 Aug;13(8):1193-202. PMID:16084391
Page seeded by OCA on Wed Nov 21 07:25:23 2007
