1hy0

CRYSTAL STRUCTURE OF WILD TYPE DUCK DELTA 1 CRYSTALLIN (EYE LENS PROTEIN)CRYSTAL STRUCTURE OF WILD TYPE DUCK DELTA 1 CRYSTALLIN (EYE LENS PROTEIN)

Structural highlights 1hy0 is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: Related: 1auw, 1dcn, 1aos Activity: Argininosuccinate lyase, with EC number 4.3.2.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ARLY1_ANAPL] Delta crystallin, the principal crystallin in embryonic lens, is found only in birds and reptiles. Despite possessing the necessary catalytic residues, this protein does not function as an enzymatically active argininosuccinate lyase. 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 Duck delta1 and delta2 crystallin are 94% identical in amino acid sequence, and while delta2 crystallin is the duck orthologue of argininosuccinate lyase (ASL) and catalyzes the reversible breakdown of argininosuccinate to arginine and fumarate, the delta1 isoform is enzymatically inactive. The crystal structures of wild type duck delta1 and delta2 crystallin have been solved at 2.2 and 2.3 A resolution, respectively, and the refinement of the turkey delta1 crystallin has been completed. These structures have been compared with two mutant duck delta2 crystallin structures. Conformational changes were observed in two regions of the N-terminal domain with intraspecies differences between the active and inactive isoforms localized to residues 23-32 and both intra- and interspecies differences localized to the loop of residues 74-89. As the residues implicated in the catalytic mechanism of delta2/ASL are all conserved in delta1, the amino acid substitutions in these two regions are hypothesized to be critical for substrate binding. A sulfate anion was found in the active site of duck delta1 crystallin. This anion, which appears to mimic the fumarate moiety of the argininosuccinate substrate, induces a rigid body movement in domain 3 and a conformational change in the loop of residues 280-290, which together would sequester the substrate from the solvent. The duck delta1 crystallin structure suggests that Ser 281, a residue strictly conserved in all members of the superfamily, could be the catalytic acid in the delta2 crystallin/ASL enzymatic mechanism. Structural studies of duck delta 1 and delta 2 crystallin suggest conformational changes occur during catalysis.,Sampaleanu LM, Vallee F, Slingsby C, Howell PL Biochemistry. 2001 Mar 6;40(9):2732-42. PMID:11258884 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Crystallin 3D structures

spinqualitylabelsall models 1hy0, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image