1at6: Difference between revisions

Revision as of 12:48, 21 February 2008

HEN EGG WHITE LYSOZYME WITH A ISOASPARTATE RESIDUE

OverviewOverview

The isomerization of Asp101 to isoaspartate autocatalytically proceeds via a succinimide intermediate in hen egg-white lysozyme at a mildly acidic condition. The crystal structures of succinimide and isoaspartate forms of the lysozyme proteins, each complexed with a tri-N-acetylchitotriose ligand, have been determined at 1.8 A resolution, and distinctively elucidate coplanar cyclic aminosuccinyl and beta-linked isoaspartyl residues. Compared with the liganded native protein with normal Asp101, succinimide 101 protrudes toward the ligand, and isoaspartate 101 extends away from the ligand. The formations of these residues caused the loss of three hydrogen-bonds between the ligand and the side-chains of Asp101 and Asn103 along with 0.5 A displacement of the ligand location.

About this StructureAbout this Structure

1AT6 is a Single protein structure of sequence from Gallus gallus. Active as Lysozyme, with EC number 3.2.1.17 Known structural/functional Site: . Full crystallographic information is available from OCA.

ReferenceReference

Succinimide and isoaspartate residues in the crystal structures of hen egg-white lysozyme complexed with tri-N-acetylchitotriose., Noguchi S, Miyawaki K, Satow Y, J Mol Biol. 1998 Apr 24;278(1):231-8. PMID:9571046

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OCA

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 ==Overview==
-The isomerization of Asp101 to isoaspartate autocatalytically proceeds via, a succinimide intermediate in hen egg-white lysozyme at a mildly acidic, condition. The crystal structures of succinimide and isoaspartate forms of, the lysozyme proteins, each complexed with a tri-N-acetylchitotriose, ligand, have been determined at 1.8 A resolution, and distinctively, elucidate coplanar cyclic aminosuccinyl and beta-linked isoaspartyl, residues. Compared with the liganded native protein with normal Asp101, succinimide 101 protrudes toward the ligand, and isoaspartate 101 extends, away from the ligand. The formations of these residues caused the loss of, three hydrogen-bonds between the ligand and the side-chains of Asp101 and, Asn103 along with 0.5 A displacement of the ligand location.
+The isomerization of Asp101 to isoaspartate autocatalytically proceeds via a succinimide intermediate in hen egg-white lysozyme at a mildly acidic condition. The crystal structures of succinimide and isoaspartate forms of the lysozyme proteins, each complexed with a tri-N-acetylchitotriose ligand, have been determined at 1.8 A resolution, and distinctively elucidate coplanar cyclic aminosuccinyl and beta-linked isoaspartyl residues. Compared with the liganded native protein with normal Asp101, succinimide 101 protrudes toward the ligand, and isoaspartate 101 extends away from the ligand. The formations of these residues caused the loss of three hydrogen-bonds between the ligand and the side-chains of Asp101 and Asn103 along with 0.5 A displacement of the ligand location.
 ==About this Structure==
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 [[Category: o-glycosyl hydrolase]]
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