1ova

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Revision as of 21:06, 20 November 2007

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spinqualitylabelsall models 1ova, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF UNCLEAVED OVALBUMIN AT 1.95 ANGSTROMS RESOLUTION

Overview

Ovalbumin, the major protein in avian egg-white, is a non-inhibitory, member of the serine protease inhibitor (serpin) superfamily. The crystal, structure of uncleaved, hen ovalbumin was solved by the molecular, replacement method using the structure of plakalbumin, a proteolytically, cleaved form of ovalbumin, as a starting model. The final refined model, including four ovalbumin molecules, 678 water molecules and a single metal, ion, has a crystallographic R-factor of 17.4% for all reflections between, 6.0 and 1.95 A resolution. The root-mean-square deviation from ideal, values in bond lengths is 0.02 A and in bond angles is 2.9 degrees. This, is the first crystal structure of a member of the serpin family in an, uncleaved form. Surprisingly, the peptide that is homologous to the, reactive centre of inhibitory serpins adopts an alpha-helical, conformation. The implications for the mechanism of inhibition of the, inhibitory members of the family is discussed.

About this Structure

1OVA is a Single protein structure of sequence from Gallus gallus with NAG, PO3, CA and ACE as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of uncleaved ovalbumin at 1.95 A resolution., Stein PE, Leslie AG, Finch JT, Carrell RW, J Mol Biol. 1991 Oct 5;221(3):941-59. PMID:1942038

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