4UFQ

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

Summary for 4UFQ

• Entry DOI: 10.2210/pdb4ufq/pdb
• Descriptor: Hyaluronidase, SULFATE ION, SODIUM ION, ... (7 entities in total)
• Functional Keywords: hydrolase
• Biological source: Streptomyces koganeiensis
• Total number of polymer chains: 2
• Total formula weight: 44837.05

Authors

Gavira, J.A.,Messina, L.,Pernagallo, S.,Unciti-Broceta, J.D.,Conejero-Muriel, M.,Diaz-Mochon, J.J.,Vaccaro, S.,Caruso, S.,Musumeci, L.,Bisicchia, S.,Di Pasquale, R. (deposition date: 2015-03-18, release date: 2016-04-13, Last modification date: 2024-10-16)

Primary citation

Messina, L.,Gavira, J.A.,Pernagallo, S.,Unciti-Broceta, J.D.,Sanchez Martin, R.M.,Diaz-Mochon, J.J.,Vaccaro, S.,Conejero-Muriel, M.,Pineda-Molina, E.,Caruso, S.,Musumeci, L.,Di Pasquale, R.,Pontillo, A.,Sincinelli, F.,Pavan, M.,Secchieri, C.
Identification and Characterization of a Bacterial Hyaluronidase and its Production in Recombinant Form.
FEBS Lett., 590:2180-, 2016

PubMed Abstract: 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 Å, 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.

PubMed: 27311405
DOI: 10.1002/1873-3468.12258

Experimental method

X-RAY DIFFRACTION (1.45 Å)