1ZFL
Solution structure of III-A, the major intermediate in the oxidative folding of leech carboxypeptidase inhibitor
Summary for 1ZFL
| Entry DOI | 10.2210/pdb1zfl/pdb |
| Related | 1DTD 1DTV 1ZFI |
| Descriptor | Metallocarboxypeptidase inhibitor (1 entity in total) |
| Functional Keywords | carboxypeptidase inhibitor, folding intermediate, oxidative folding, four-stranded antiparallel beta-sheet, hydrolase inhibitor |
| Biological source | Hirudo medicinalis (medicinal leech) |
| Total number of polymer chains | 1 |
| Total formula weight | 7397.26 |
| Authors | Arolas, J.L.,D'Silva, L.,Popowicz, G.M.,Aviles, F.X.,Holak, T.A.,Ventura, S. (deposition date: 2005-04-20, release date: 2005-09-13, Last modification date: 2024-11-20) |
| Primary citation | Arolas, J.L.,D'Silva, L.,Popowicz, G.M.,Aviles, F.X.,Holak, T.A.,Ventura, S. NMR structural characterization and computational predictions of the major intermediate in oxidative folding of leech carboxypeptidase inhibitor STRUCTURE, 13:1193-1202, 2005 Cited by PubMed Abstract: 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. PubMed: 16084391DOI: 10.1016/j.str.2005.05.008 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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