1OVA

CRYSTAL STRUCTURE OF UNCLEAVED OVALBUMIN AT 1.95 ANGSTROMS RESOLUTION

Summary for 1OVA

• Entry DOI: 10.2210/pdb1ova/pdb
• Descriptor: OVALBUMIN, 2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (6 entities in total)
• Functional Keywords: serpin
• Biological source: Gallus gallus (chicken); More
• Cellular location: Secreted: P01012 P01012 P01012
• Total number of polymer chains: 4
• Total formula weight: 172436.65

Authors

Stein, P.E.,Leslie, A.G.W. (deposition date: 1990-11-26, release date: 1992-04-15, Last modification date: 2024-10-30)

Primary citation

Stein, P.E.,Leslie, A.G.,Finch, J.T.,Carrell, R.W.
Crystal structure of uncleaved ovalbumin at 1.95 A resolution.
J.Mol.Biol., 221:941-959, 1991

PubMed Abstract: 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.

PubMed: 1942038
DOI: 10.1016/0022-2836(91)80185-W

Experimental method

X-RAY DIFFRACTION (1.95 Å)