1o9j

The X-ray crystal structure of eta-crystallinThe X-ray crystal structure of eta-crystallin

Structural highlights 1o9j is a 4 chain structure with sequence from Elephantulus edwardii. The May 2007 RCSB PDB Molecule of the Month feature on Aconitase and Iron Regulatory Protein 1 by David S. Goodsell is 10.2210/rcsb_pdb/mom_2007_5. The July 2010 RCSB PDB Molecule of the Month feature on Crystallins by David Goodsell is 10.2210/rcsb_pdb/mom_2010_7. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.4Å Ligands: , , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ALDH1_ELEED Major component of the eye of elephant shrews, which in contrast to other mammals, possesses both a lens- and a non-lens class-1 aldehyde dehydrogenase 1. This eye-specific form is a structural protein of the lens and, in other part of the eye, serves as the major form of ALDH1. Can convert/oxidize retinaldehyde to retinoic acid. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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 there are some mutations to the substrate access tunnel that might affect binding or release of substrate and product. It is possible that eta-crystallin has lost flexibility to improve its role in the lens. Enhanced binding of cofactor could enable it to act as a UV/blue light filter in the lens, improving visual acuity. The structure not only gives a view of a "natural mutant" of ALDH1 illustrating the adaptive conflict that can arise in multifunctional proteins, but also provides a well-ordered NAD binding site structure for this class of enzymes with important roles in development and health. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aldehyde dehydrogenase Aldehyde dehydrogenase 3D structures

spinqualitylabelsall models 1o9j, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image