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Structure paper

TitleEnzyme-ligand interactions that drive active site rearrangements in the Helicobacter pylori 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase.
Journal, issue, pagesProtein Sci., Vol. 19, Page 2498-2510, Year 2010
Publish dateJun 21, 2010 (structure data deposition date)
AuthorsRonning, D.R. / Iacopelli, N.M. / Mishra, V.
External linksProtein Sci. / PubMed:20954236
MethodsX-ray diffraction
Resolution1.602 - 1.8 Å
Structure data

PDB-3nm4:
Helicobacter pylori MTAN
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-3nm5:
Helicobacter pylori MTAN complexed with Formycin A
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-3nm6:
Helicobacter pylori MTAN complexed with adenine and tris
Method: X-RAY DIFFRACTION / Resolution: 1.602 Å

Chemicals

ChemComp-TRS:
2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

ChemComp-FMC:
(1S)-1-(7-amino-1H-pyrazolo[4,3-d]pyrimidin-3-yl)-1,4-anhydro-D-ribitol

ChemComp-ADE:
ADENINE

Source
  • helicobacter pylori (bacteria)
KeywordsHYDROLASE / nucleosidase

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