1at6
From Proteopedia
(New page: 200px<br /> <applet load="1at6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1at6, resolution 1.80Å" /> '''HEN EGG WHITE LYSOZ...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1AT6 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/ ]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AT6 OCA]]. | + | 1AT6 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]]. Active as [[http://en.wikipedia.org/wiki/Lysozyme Lysozyme]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17]]. Structure known Active Site: IAS. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AT6 OCA]]. |
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9571046 9571046] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9571046 9571046] | ||
| + | [[Category: Gallus gallus]] | ||
| + | [[Category: Lysozyme]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Miyawaki, K.]] | [[Category: Miyawaki, K.]] | ||
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[[Category: o-glycosyl hydrolase]] | [[Category: o-glycosyl hydrolase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:59:12 2007'' |
Revision as of 10:54, 30 October 2007
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HEN EGG WHITE LYSOZYME WITH A ISOASPARTATE RESIDUE
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.
About this Structure
1AT6 is a [Single protein] structure of sequence from [Gallus gallus]. Active as [Lysozyme], with EC number [3.2.1.17]. Structure known Active Site: IAS. 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
Page seeded by OCA on Tue Oct 30 12:59:12 2007
