1A90

RECOMBINANT MUTANT CHICKEN EGG WHITE CYSTATIN, NMR, 31 STRUCTURES

Summary for 1A90

• Entry DOI: 10.2210/pdb1a90/pdb
• Descriptor: CYSTATIN (1 entity in total)
• Functional Keywords: proteinase inhibitor, thiol proteinase, steffins, kininogens, thiol protease inhibitor
• Biological source: Gallus gallus (chicken)
• Cellular location: Secreted: P01038
• Total number of polymer chains: 1
• Total formula weight: 12168.79

Authors

Dieckmann, T.,Mitschang, L.,Hofmann, M.,Kos, J.,Turk, V.,Auerswald, E.A.,Jaenicke, R.,Oschkinat, H. (deposition date: 1998-04-14, release date: 1998-06-17, Last modification date: 2024-10-30)

Primary citation

Dieckmann, T.,Mitschang, L.,Hofmann, M.,Kos, J.,Turk, V.,Auerswald, E.A.,Jaenicke, R.,Oschkinat, H.
The structures of native phosphorylated chicken cystatin and of a recombinant unphosphorylated variant in solution.
J.Mol.Biol., 234:1048-1059, 1993

PubMed Abstract: The solution structures of the phosphorylated form of native chicken cystatin and the recombinant variant AEF-S1M-M29I-M89L were determined by 2D, 3D and 4D-NMR. The structures turn out to be very similar, despite the substitutions and the phosphorylation of the wild-type. Their dominant feature is a five-stranded beta-sheet, which is wrapped around a five-turn alpha-helix, as shown by X-ray crystallographic studies of wild-type chicken cystatin. However, the NMR analysis shows that the second helix observed in the crystal is not present in solution. The phosphorylation occurs at S80, which is located in a flexible region. For this reason, very few effects on the structure are observed. Comparison of structures of the unphosphorylated variant and the wild-type shows small effects on H84 which is located in the supposed recognition site of the serine kinase. This recognition site appears to be well structured as a large loop-containing bulge of the beta-sheet. The N termini of both mutants, which contribute to a large extent to the binding to the proteinase, are very flexible. A loop structure involving the residues L7 to A10 as found in related inhibitors, such as in the kininogen domains 2 and 3, is not sufficiently populated to be observed.

PubMed: 8263912
DOI: 10.1006/jmbi.1993.1658

Experimental method

SOLUTION NMR