4ufq

Structure of a novel Hyaluronidase (Hyal_Sk) from Streptomyces koganeiensis.

spinqualitylabelsall models 4ufq, resolution 1.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ufq is a 2 chain structure with sequence from Streptomyces koganeiensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.45Å Ligands: CL, GOL, MSE, NA, PEG, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0U2E2J7_9ACTN Publication Abstract from PubMed Hyaluronidases (Hyals) are broadly used in medical applications to facilitate the dispersion and/or absorption of fluids or medications. This study reports the isolation, cloning, and industrial-scale recombinant production, purification and full characterization, including X-ray structure determination at 1.45 A, of an extracellular Hyal from the nonpathogenic bacterium Streptomyces koganeiensis. The recombinant S. koganeiensis Hyal (rHyal_Sk) has a novel bacterial catalytic domain with high enzymatic activity, compared with commercially available Hyals, and is more thermostable and presents higher proteolytic resistance, with activity over a broad pH range. Moreover, rHyal_Sk exhibits remarkable substrate specificity for hyaluronic acid (HA) and poses no risk of animal cross-infection. Identification and characterization of a bacterial hyaluronidase and its production in recombinant form.,Messina L, Gavira JA, Pernagallo S, Unciti-Broceta JD, Sanchez Martin RM, Diaz-Mochon JJ, Vaccaro S, Conejero-Muriel M, Pineda-Molina E, Caruso S, Musumeci L, Di Pasquale R, Pontillo A, Sincinelli F, Pavan M, Secchieri C FEBS Lett. 2016 Jun 17. doi: 10.1002/1873-3468.12258. PMID:27311405 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Hyaluronidase 3D structures

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