1at5: Difference between revisions

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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: succinimide]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:48:02 2008''

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@@ Line 4: / Line 4: @@
 ==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==
@@ Line 23: / Line 23: @@
 [[Category: succinimide]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:31:31 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:48:02 2008''