TAILIEUCHUNG - Báo cáo khoa học: Structural and mutational analysis of TenA protein (HP1287) from the Helicobacter pylori thiamin salvage pathway – evidence of a different substrate specificity

Structural and mutational analysis of TenA protein (HP1287) from the Helicobacter pylori thiamin salvage pathway – evidence of a different substrate specificity Nicola Barison1,2, Laura Cendron1,2, Alberto Trento2, Alessandro Angelini2,* and Giuseppe Zanotti1,2,3 1 Department of Biological Chemistry, University of Padua, Italy 2 Venetian Institute of Molecular Medicine (VIMM), Padua, Italy 3 Institute of Biomolecular Chemistry of CNR, Padua, Italy Keywords Helicobacter pylori; stomach colonization; thiamin; thiaminase; vitamin B1 Correspondence G. Zanotti, Department of Biological Chemistry, University of Padua, Viale G. Colombo 3, 35121 Padova, Italy Fax: +39 049 8073310 Tel: +39 049 8276409 E-mail: *Present address Laboratory of Therapeutic Proteins and. | ỊFEBS Journal Structural and mutational analysis of TenA protein HP1287 from the Helicobacter pylori thiamin salvage pathway - evidence of a different substrate specificity Nicola Barison1 2 Laura Cendron1 2 Alberto Trento2 Alessandro Angelini2 and Giuseppe Zanotti1 2 3 1 Department of BiologicalChemistry University of Padua Italy 2 Venetian Institute of Molecular Medicine VIMM Padua Italy 3 Institute of Biomolecular Chemistry of CNR Padua Italy Keywords Helicobacter pylori stomach colonization thiamin thiaminase vitamin B1 Correspondence G. Zanotti Department of Biological Chemistry University of Padua Viale G. Colombo 3 35121 Padova Italy Fax 39 049 8073310 Tel 39 049 8276409 E-mail Present address Laboratory of Therapeutic Proteins and Peptides-LPPT Institute of Chemical Sciences and Engineering Ecole Polytechnique Federalde Lausanne EPFL Lausanne Switzerland Database Coordinates have been deposited in the Protein Data Bank with accession codes 2RD3 and 3IBX. UniProtKB TrEMBL accession number O25874 A8KRL3 Received 20 July 2009 revised 17 August 2009 accepted 24 August 2009 doi HP1287 tenA from Helicobacter pylori is included among the genes that play a relevant role in bacterium colonization and persistence. The gene has been cloned and its product protein TenA has been expressed and purified. The crystal structures of the wild-type protein and the mutant F47Y have been determined at resolutions of and A respectively. The molecular model a homotetramer with 222 symmetry shows that the H. pylori TenA structure belongs to the thiaminase II class of proteins. These enzymes were recently found to be involved in a salvage pathway for the synthesis of the thiamin precursor hydroxypyrimidine which constitutes a building block in thiamin biosynthesis in particular in bacteria living in the soil. By contrast enzymatic measurements on TenA from H. pylori indicate that the activity on the putative .

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