1at6: Difference between revisions
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[[Image:1at6.gif|left|200px]]<br /> | [[Image:1at6.gif|left|200px]]<br /><applet load="1at6" size="450" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1at6" size="450" color="white" frame="true" align="right" spinBox="true" | |||
caption="1at6, resolution 1.80Å" /> | caption="1at6, resolution 1.80Å" /> | ||
'''HEN EGG WHITE LYSOZYME WITH A ISOASPARTATE RESIDUE'''<br /> | '''HEN EGG WHITE LYSOZYME WITH A ISOASPARTATE RESIDUE'''<br /> | ||
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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/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] | 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] Known structural/functional Site: <scene name='pdbsite=IAS:ASP 101 Isomerized To Isoaspartate'>IAS</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AT6 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: o-glycosyl hydrolase]] | [[Category: o-glycosyl hydrolase]] | ||
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Revision as of 15:11, 18 December 2007
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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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