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PDBsum entry 1ova
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structure of uncleaved ovalbumin at 1.95 a resolution.
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Authors
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P.E.Stein,
A.G.Leslie,
J.T.Finch,
R.W.Carrell.
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Ref.
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J Mol Biol, 1991,
221,
941-959.
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PubMed id
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Abstract
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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.
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Secondary reference #1
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Title
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Crystal structure of ovalbumin as a model for the reactive centre of serpins.
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Authors
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P.E.Stein,
A.G.Leslie,
J.T.Finch,
W.G.Turnell,
P.J.Mclaughlin,
R.W.Carrell.
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Ref.
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Nature, 1990,
347,
99.
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PubMed id
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