Enzyme-ligand interactions that drive active site rearrangements in the Helicobacter pylori 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase. | Protein Sci;19(12): 2498-510, 2010 Dec. | MEDLINE

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Enzyme-ligand interactions that drive active site rearrangements in the Helicobacter pylori 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase.

Ronning, Donald R; Iacopelli, Natalie M; Mishra, Vidhi.

Affiliation

Ronning DR; Department of Chemistry, University of Toledo, Toledo, Ohio 43606, USA. donald.ronning@utoledo.edu

Protein Sci ; 19(12): 2498-510, 2010 Dec.

Article in En | MEDLINE | ID: mdl-20954236

Subject(s)

Helicobacter pylori/enzymology; N-Glycosyl Hydrolases/chemistry; N-Glycosyl Hydrolases/metabolism; Catalytic Domain; Crystallography, X-Ray; Molecular Structure; Protein Binding; Quorum Sensing

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Helicobacter pylori / N-Glycosyl Hydrolases Language: En Journal: Protein Sci Year: 2010 Document type: Article

Search on Google

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Helicobacter pylori / N-Glycosyl Hydrolases Language: En Journal: Protein Sci Year: 2010 Document type: Article