TAILIEUCHUNG - Báo cáo khoa học: Polysaccharide binding sites in hyaluronate lyase – crystal structures of native phage–encoded hyaluronate lyase and its complexes with ascorbic acid and lactose

Hyaluronate lyases are a class of endoglycosaminidase enzymes with a high level of complexity and heterogeneity. The main function of the Streptococ-cus pyogenesbacteriophage protein hyaluronate lyase, HylP2, is to degrade hyaluronan into unsaturated disaccharide units. HylP2 was cloned, over-expressed and purified to homogeneity. | Polysaccharide binding sites in hyaluronate lyase - crystal structures of native phage-encoded hyaluronate lyase and its complexes with ascorbic acid and lactose Parul Mishra R. Prem Kumar2 z Abdul S. Ethayathulla2 Nagendra Singh2 Sujata Sharma2 Markus Perbandt3 Christian Betzel3 Punit Kaur2 Alagiri Srinivasan2 Vinod Bhakuni1 and Tej P. Singh2 1 Department of Molecular and StructuralBiology CentralDrug Research Institute Lucknow India 2 Department of Biophysics All India Institute of MedicalSciences New Delhi India 3 Department of Biochemistry and Molecular Biology University of Hamburg Germany Keywords ascorbic acid complex hyaluranidase HylP2 lactose complex triple-stranded b-helix Correspondence T. P. Singh Department of Biophysics All India Institute of MedicalSciences Ansari Nagar New Delhi 110 029 India Fax 91 11 2658 8663 Tel 91 11 2658 8931 E-mail Database Atomic coordinates have been deposited in the Protein Data Bank as entries 2YW0 native 3EKA ascorbic acid complex and 2YVV lactose complex These authors contributed equally to this work Received 24 November 2008 revised 11 April2009 accepted 17 April2009 doi Hyaluronate lyases are a class of endoglycosaminidase enzymes with a high level of complexity and heterogeneity. The main function of the Streptococcus pyogenes bacteriophage protein hyaluronate lyase HylP2 is to degrade hyaluronan into unsaturated disaccharide units. HylP2 was cloned overexpressed and purified to homogeneity. The recombinant HylP2 exists as a homotrimer with a molecular mass of approximately 110 kDa under physiological conditions. The HylP2 was crystallized and the crystals were soaked in two separate reservoir solutions containing ascorbic acid and lactose respectively. The crystal structures of native HylP2 and its two complexes with ascorbic acid and lactose have been determined. HylP2 folds into four distinct domains with a central core consisting of 16 antiparallel .

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