3lqb | pdb_00003lqb

Crystal structure of the hatching enzyme ZHE1 from the zebrafish Danio rerio

spinqualitylabelsall models 3lqb, resolution 1.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3lqb is a 1 chain structure with sequence from Danio rerio. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.1Å Ligands: EDO, SO4, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function HE12_DANRE Metalloendopeptidase which participates in the breakdown of the egg envelope at the time of hatching. Cleaves the N-terminal regions of the zona pellucia glycoproteins ZP2 and ZP3, where it specifically recognizes the peptide sequences TVQQS-|-DYLIK (major site) and KLMLK-|-APEPF (minor site). 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 Fish hatching enzymes are zinc metalloproteases that digest the egg envelope (chorion) at the time of hatching. The crystal structure of zebrafish hatching enzyme 1 (ZHE1) has been solved at 1.10 A resolution. ZHE1 is monomeric, is mitten shaped, and has a cleft at the center of the molecule. ZHE1 consists of three 3(10)-helices, three alpha-helices, and two beta-sheets. The central cleft represents the active site of the enzyme that is crucial for substrate recognition and catalysis. Alanine-scanning mutagenesis of the two substrate peptides has shown that AspP1' contributes the most and that the residues at P4-P2' also contribute to the recognition of the major substrate peptide by ZHE1, whereas GluP3' and the hydrophobic residues at P4-P2, P2', and P5' contribute significantly to the recognition of the minor substrate peptide by ZHE1. Molecular models of these two substrate peptides bound to ZHE1 have been built based on the crystal structure of a transition-state analog inhibitor bound to astacin. In substrate-recognition models, the AspP1' in the major substrate peptide forms a salt bridge with Arg182 of ZHE1, while the GluP3' in the minor substrate peptide instead forms a salt bridge with Arg182. Thus, these two substrate peptides would be differently recognized by ZHE1. The shapes and electrostatic potentials of the substrate-binding clefts of ZHE1 and the structurally similar proteins astacin and bone morphogenetic protein 1 are significantly dissimilar due to different side chains, which would confer their distinctive substrate preferences. Crystal Structure of Zebrafish Hatching Enzyme 1 from the Zebrafish Danio rerio.,Okada A, Sano K, Nagata K, Yasumasu S, Ohtsuka J, Yamamura A, Kubota K, Iuchi I, Tanokura M J Mol Biol. 2010 Aug 18. PMID:20727360 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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