1at5: Difference between revisions

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[[Image:1at5.~~gif~~|left|200px]]

[[Image:1at5.png|left|200px]]

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~~'''~~HEN EGG WHITE LYSOZYME WITH A SUCCINIMIDE RESIDUE~~'''~~

===HEN EGG WHITE LYSOZYME WITH A SUCCINIMIDE RESIDUE===

~~==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.~~

The line below this paragraph, {{ABSTRACT_PUBMED_9571046}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 9571046 is the PubMed ID number.

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==About this Structure==

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[[Category: O-glycosyl hydrolase]]

[[Category: Succinimide]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 10~~:39:57 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:33:04 2008''

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-[[Image:1at5.gif|left|200px]]
+{{Seed}}
+[[Image:1at5.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1at5|  PDB=1at5  |  SCENE=  }}
-'''HEN EGG WHITE LYSOZYME WITH A SUCCINIMIDE RESIDUE'''
+===HEN EGG WHITE LYSOZYME WITH A SUCCINIMIDE 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.
+The line below this paragraph, {{ABSTRACT_PUBMED_9571046}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9571046 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9571046}}
 ==About this Structure==
@@ Line 29: / Line 33: @@
 [[Category: O-glycosyl hydrolase]]
 [[Category: Succinimide]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 10:39:57 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:33:04 2008''