A LEFT-HANDED CROSSOVER INVOLVED IN AMIDOHYDROLASE CATALYSIS - CRYSTAL-STRUCTURE OF ERWINIA-CHRYSANTHEMI L-ASPARAGINASE WITH BOUND L-ASPARTATE

被引:80
作者
MILLER, M
RAO, JKM
WLODAWER, A
GRIBSKOV, MR
机构
[1] Macromolecular Structure Laboratory, NCI-FCRDC, ABL-Basic Research Program, Frederick
关键词
L-ASPARAGINASE; LEFT-HANDED CROSSOVER; CRYSTAL STRUCTURE; L-ASPARTATE-BOUND AMIDOHYDROLASE; THREONINE AS NUCLEOPHILE; ERWINIA-CHRYSANTHEMI;
D O I
10.1016/0014-5793(93)80943-O
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The crystal structure of L-asparaginase from Erwinia chrysanthemi in the presence and absence Of L-aspartate was determined at 1.8 angstrom resolution. Conserved residues in a left-handed crossover (a rare occurrence in protein structures) link pairs of dimers into the catalytically active tetrameric form of the enzyme. The structure of ErA containing bound aspartic acid shows that this unusual strand connectivity is an essential part of the active site architecture, responsible for releasing the product of the enzymatic hydrolysis. The orientation of the bound aspartate indicates for the first time a threonine residue as a catalytic nucleophile.
引用
收藏
页码:275 / 279
页数:5
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