2zof | pdb_00002zof

Crystal structure of mouse carnosinase CN2 complexed with MN and bestatin

spinqualitylabelsall models 2zof, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2zof is a 2 chain structure with sequence from Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BES, MN Related: 2zog Gene: Cndp2, Cn2 (LK3 transgenic mice) Activity: Cytosol nonspecific dipeptidase, with EC number 3.4.13.18 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CNDP2_MOUSE] Hydrolyzes a variety of dipeptides including L-carnosine. Has a strong preference for Cys-Gly (By similarity). 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 L-carnosine is a bioactive dipeptide (beta-alanyl-L-histidine) present in mammalian tissues, including the central nervous system, and has potential neuroprotective and neurotransmitter functions. In mammals, two types of L-carnosine-hydrolyzing enzymes (CN1 and CN2) have been cloned thus far, and they have been classified as metallopeptidases of the M20 family. The enzymatic activity of CN2 requires Mn(2+), and CN2 is inhibited by a nonhydrolyzable substrate analog, bestatin. Here, we present the crystal structures of mouse CN2 complexed with bestatin together with Zn(2+) at a resolution of 1.7 A and that with Mn(2+) at 2.3 A CN2 is a homodimer in a noncrystallographic asymmetric unit, and the Mn(2+) and Zn(2+) complexes closely resemble each other in the overall structure. Each subunit is composed of two domains: domain A, which is complexed with bestatin and two metal ions, and domain B, which provides the major interface for dimer formation. The bestatin molecule bound to domain A interacts with several residues of domain B of the other subunit, and these interactions are likely to be essential for enzyme activity. Since the bestatin molecule is not accessible to the bulk water, substrate binding would require conformational flexibility between domains A and B. The active site structure and substrate-binding model provide a structural basis for the enzymatic activity and substrate specificity of CN2 and related enzymes. Structural basis for substrate recognition and hydrolysis by mouse carnosinase CN2.,Unno H, Yamashita T, Ujita S, Okumura N, Otani H, Okumura A, Nagai K, Kusunoki M J Biol Chem. 2008 Oct 3;283(40):27289-99. Epub 2008 Jun 12. PMID:18550540 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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