1at6

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{{STRUCTURE_1at6| PDB=1at6 | SCENE= }}
{{STRUCTURE_1at6| PDB=1at6 | SCENE= }}
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'''HEN EGG WHITE LYSOZYME WITH A ISOASPARTATE RESIDUE'''
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===HEN EGG WHITE LYSOZYME WITH A ISOASPARTATE RESIDUE===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_9571046}}
==About this Structure==
==About this Structure==
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[[Category: Isoaspartate]]
[[Category: Isoaspartate]]
[[Category: O-glycosyl hydrolase]]
[[Category: O-glycosyl hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:33:08 2008''

Revision as of 14:33, 30 June 2008

Image:1at6.png

Template:STRUCTURE 1at6

HEN EGG WHITE LYSOZYME WITH A ISOASPARTATE RESIDUE

Template:ABSTRACT PUBMED 9571046

About this Structure

1AT6 is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

Reference

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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