1o9j
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THE X-RAY CRYSTAL STRUCTURE OF ETA-CRYSTALLIN
OverviewOverview
Eta-crystallin is a retinal dehydrogenase that has acquired a role as a, structural protein in the eye lens of elephant shrews, members of an, ancient order of mammals. While it retains some activity toward retinal, which is oxidized to retinoic acid, the protein has acquired a number of, specific sequence changes that have presumably been selected to enhance, the lens role. The crystal structure of eta-crystallin, in common with, class 1 and 2 ALDHs, is a dimer of dimers. It has a better-defined NAD, binding site than those of related mammalian ALDH1 enzymes with the, cofactor bound in the "hydride transfer" position in all four monomers, with small differences about the dimer dyads. Although the active site is, well conserved, the substrate-binding site is larger in eta-crystallin, and ... [(full description)]
About this StructureAbout this Structure
1O9J is a [Single protein] structure of sequence from [Elephantulus edwardii] with NAD, DTT and DTU as [ligands]. The following page contains interesting information on the relation of 1O9J with [Aconitase and Iron Regulatory Protein 1]. Active as [[1]], with EC number [1.2.1.3]. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal structure of eta-crystallin: adaptation of a class 1 aldehyde dehydrogenase for a new role in the eye lens., Bateman OA, Purkiss AG, van Montfort R, Slingsby C, Graham C, Wistow G, Biochemistry. 2003 Apr 22;42(15):4349-56. PMID:12693930
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