1ova

CRYSTAL STRUCTURE OF UNCLEAVED OVALBUMIN AT 1.95 ANGSTROMS RESOLUTION

spinqualitylabelsall models 1ova, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ova is a 4 chain structure with sequence from Chick. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, NAG NonStd Res: ACE, SEP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [OVAL_CHICK] Non-inhibitory serpin. Storage protein of egg white. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ovalbumin

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