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Structure paper

TitleBiochemical and Structural Studies of 6-Carboxy-5,6,7,8-tetrahydropterin Synthase Reveal the Molecular Basis of Catalytic Promiscuity within the Tunnel-fold Superfamily.
Journal, issue, pagesJ. Biol. Chem., Vol. 289, Page 23641-23652, Year 2014
Publish dateDec 2, 2013 (structure data deposition date)
AuthorsMiles, Z.D. / Roberts, S.A. / McCarty, R.M. / Bandarian, V.
External linksJ. Biol. Chem. / PubMed:24990950
MethodsX-ray diffraction
Resolution1.6 - 2.05 Å
Structure data

PDB-4ntk:
QueD from E. coli
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

PDB-4ntm:
QueD soaked with sepiapterin (selenomethionine substituted protein)
Method: X-RAY DIFFRACTION / Resolution: 2.05 Å

PDB-4ntn:
E.coli QueD, SeMet protein, 2A resolution
Method: X-RAY DIFFRACTION / Resolution: 1.99 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-ZSP:
2-amino-6-[(1Z)-1,2-dihydroxyprop-1-en-1-yl]-7,8-dihydropteridin-4(3H)-one

ChemComp-ACT:
ACETATE ION

ChemComp-HOH:
WATER

ChemComp-2K8:
(6R)-2-amino-4-oxo-3,4,5,6,7,8-hexahydropteridine-6-carboxylic acid

ChemComp-FMT:
FORMIC ACID

Source
  • escherichia coli (E. coli)
KeywordsLYASE / T-fold / 6-PTPS / queuosine biosynthesis enzyme / sepiapterin / C27A

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