1jti
From Proteopedia
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| , resolution 2.30Å | |||||||
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| Gene: | ovalbumin (Gallus gallus) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Loop-inserted Structure of P1-P1' Cleaved Ovalbumin Mutant R339T
Overview
Ovalbumin is a member of a superfamily of serine proteinase inhibitors, known as the serpins. It is, however, non-inhibitory towards serine proteinases, and lacks the loop insertion mechanism common to the serpins due to unknown structural factors. Mutant ovalbumin, R339T, in which the P14 hinge residue is replaced, was produced and analyzed for its thermostability and three-dimensional structure. Differential scanning calorimetry revealed that the mutant ovalbumin, but not the wild-type protein, undergoes a marked thermostabilization (DeltaT(m)=15.8 degrees C) following the P1-P1' cleavage. Furthermore, the crystal structure, solved at 2.3 A resolution, clearly proved that the P1-P1' cleaved form assumes the fully loop-inserted conformation as seen in serpin that possess inhibitory activity. We therefore conclude that ovalbumin acquires the structural transition mechanism into the loop-inserted, thermostabilized form by the single hinge mutation. The mutant protein does not, however, possess inhibitory activity. The solved structure displays the occurrence of specific interactions that may prevent the smooth motion, relative to sheet A, of helices E and F and of the loop that follows helix F. These observations provide crucial insights into the question why R339T is still non-inhibitory.
About this Structure
1JTI is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
Reference
Loop-inserted and thermostabilized structure of P1-P1' cleaved ovalbumin mutant R339T., Yamasaki M, Arii Y, Mikami B, Hirose M, J Mol Biol. 2002 Jan 11;315(2):113-20. PMID:11779232
Page seeded by OCA on Sun Mar 30 21:38:47 2008
