1fcv

CRYSTAL STRUCTURE OF BEE VENOM HYALURONIDASE IN COMPLEX WITH HYALURONIC ACID TETRAMER

spinqualitylabelsall models 1fcv, resolution 2.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1fcv is a 1 chain structure with sequence from Apime. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GCU, NAG Related: 1fcq, 1fcu Activity: Hydrolase, with EC number 3.2.1.35 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [HUGA_APIME] Hydrolyzes high molecular weight hyaluronic acid to produce small oligosaccharides (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 BACKGROUND: Hyaluronic acid (HA) is the most abundant glycosaminoglycan of vertebrate extracellular spaces and is specifically degraded by a beta-1,4 glycosidase. Bee venom hyaluronidase (Hya) shares 30% sequence identity with human hyaluronidases, which are involved in fertilization and the turnover of HA. On the basis of sequence similarity, mammalian enzymes and Hya are assigned to glycosidase family 56 for which no structure has been reported yet. RESULTS: The crystal structure of recombinant (Baculovirus) Hya was determined at 1.6 A resolution. The overall topology resembles a classical (beta/alpha)(8) TIM barrel except that the barrel is composed of only seven strands. A long substrate binding groove extends across the C-terminal end of the barrel. Cocrystallization with a substrate analog revealed the presence of a HA tetramer bound to subsites -4 to -1 and distortion of the -1 sugar. CONCLUSIONS: The structure of the complex strongly suggest an acid-base catalytic mechanism, in which Glu113 acts as the proton donor and the N-acetyl group of the substrate is the nucleophile. The location of the catalytic residues shows striking similarity to bacterial chitinase which also operates via a substrate-assisted mechanism. Crystal structure of hyaluronidase, a major allergen of bee venom.,Markovic-Housley Z, Miglierini G, Soldatova L, Rizkallah PJ, Muller U, Schirmer T Structure. 2000 Oct 15;8(10):1025-35. PMID:11080624 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Hyaluronidase 3D structures

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