1ova

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(New page: 200px<br /><applet load="1ova" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ova, resolution 1.95&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1ova.gif|left|200px]]<br /><applet load="1ova" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ova.gif|left|200px]]<br /><applet load="1ova" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ova, resolution 1.95&Aring;" />
caption="1ova, resolution 1.95&Aring;" />
'''CRYSTAL STRUCTURE OF UNCLEAVED OVALBUMIN AT 1.95 ANGSTROMS RESOLUTION'''<br />
'''CRYSTAL STRUCTURE OF UNCLEAVED OVALBUMIN AT 1.95 ANGSTROMS RESOLUTION'''<br />
==Overview==
==Overview==
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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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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==
==About this Structure==
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1OVA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with NAG, PO3, CA and ACE as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OVA OCA].
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1OVA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=PO3:'>PO3</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=ACE:'>ACE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OVA OCA].
==Reference==
==Reference==
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[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Leslie, A.G.W.]]
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[[Category: Leslie, A G.W.]]
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[[Category: Stein, P.E.]]
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[[Category: Stein, P E.]]
[[Category: ACE]]
[[Category: ACE]]
[[Category: CA]]
[[Category: CA]]
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[[Category: serpin]]
[[Category: serpin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:13:28 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:21:56 2008''

Revision as of 12:21, 21 February 2008


1ova, resolution 1.95Å

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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 , , and 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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