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Structure paper

TitleThe structure of glucose-1-phosphate thymidylyltransferase from Mycobacterium tuberculosis reveals the location of an essential magnesium ion in the RmlA-type enzymes.
Journal, issue, pagesProtein Sci., Vol. 27, Page 441-450, Year 2018
Publish dateSep 29, 2017 (structure data deposition date)
AuthorsBrown, H.A. / Thoden, J.B. / Tipton, P.A. / Holden, H.M.
External linksProtein Sci. / PubMed:29076563
MethodsX-ray diffraction
Resolution1.6 - 1.85 Å
Structure data

PDB-6b5e:
Mycobacterium tuberculosis RmlA in complex with dTDP-glucose
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

PDB-6b5k:
Mycobacterium tuberculosis RmlA in complex with Mg/dTTP
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

Chemicals

ChemComp-DAU:
2'DEOXY-THYMIDINE-5'-DIPHOSPHO-ALPHA-D-GLUCOSE

ChemComp-MG:
Unknown entry

ChemComp-TYD:
THYMIDINE-5'-DIPHOSPHATE

ChemComp-CL:
Unknown entry

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-NA:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-TTP:
THYMIDINE-5'-TRIPHOSPHATE

Source
  • mycobacterium tuberculosis (strain atcc 25618 / h37rv) (bacteria)
KeywordsTRANSFERASE / nucleotidyltransferase / product / sugar-modifying / substrate

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