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Nat Struct Biol. 1994 Oct;1(10):724-34.

The structure of avian eye lens delta-crystallin reveals a new fold for a superfamily of oligomeric enzymes.

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1
Laboratory of Molecular Biology, Birkbeck College, London, UK.

Erratum in

  • Nat Struct Biol 1994 Nov;1(11):831.

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.

Comment in

PMID:
7634077
[Indexed for MEDLINE]

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