| Literature DB >> 7634077 |
A Simpson1, O Bateman, H Driessen, P Lindley, D Moss, S Mylvaganam, E Narebor, C Slingsby.
Abstract
The crystal structure of turkey delta-crystallin, a principal soluble components of the avian lens, has been determined to a resolution of 2.5 A. It is a tetramer, of 200,000 M(r), with 222 symmetry. The subunit has a new fold composed of three mainly alpha-helical domains. One domain is a bundle of five long helices which forms a 20-helix bundle at the core of the tetramer. delta-crystallin shares 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-muconate 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.Entities:
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Year: 1994 PMID： 7634077 DOI： 10.1038/nsb1094-724
Source DB: PubMed Journal: Nat Struct Biol ISSN： 1072-8368