THE STRUCTURE OF AVIAN EYE LENS DELTA-CRYSTALLIN REVEALS A NEW FOLD FOR A SUPERFAMILY OF OLIGOMERIC ENZYMES

被引:70
作者
SIMPSON, A
BATEMAN, O
DRIESSEN, H
LINDLEY, P
MOSS, D
MYLVAGANAM, S
NAREBOR, E
SLINGSBY, C
机构
[1] UNIV LONDON BIRKBECK COLL,DEPT CRYSTALLOG,IMPERIAL CANC RES FUND UNIT,LONDON WC1E 7HX,ENGLAND
[2] DRAL,DARESBURY LAB,WARRINGTON WA4 4AD,CHESHIRE,ENGLAND
来源
NATURE STRUCTURAL BIOLOGY | 1994年 / 1卷 / 10期
关键词
D O I
10.1038/nsb1094-724
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 turkey delta-crystallin, a principal soluble components of the avian lens, has been determined to a resolution of 2.5 Angstrom. It is a tetramer, of 200,000 M(1), with 222 symmetry. The subunit has a new fold composed of three mainly a-helical domains. One domain is a bundle of five long helices which forms a 2O-helix bundle at the cove of the tetramer. delta-crystallin shaves approximately 90% sequence identity with the enzyme argininosuccinate lyase (EC 4.3.2.1), indicating that it is an example of a 'hijacked' enzyme. It is also distantly related to the class II fumarases, aspartases, adenylosuccinases and 3-carboxy-cis,cis-mueonate lactonising enzyme. The structure reveals a putative active-site cleft which is located on the boundary between three subunits of the tetramer. This is the first three-dimensional structure of a representative of this superfamily of enzymes.
引用
收藏
页码:724 / 734
页数:11
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