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Structure paper

TitleThe GDP-switched GAF domain of DcpA modulates the concerted synthesis/hydrolysis of c-di-GMP inMycobacterium smegmatis.
Journal, issue, pagesBiochem. J., Vol. 475, Page 1295-1308, Year 2018
Publish dateNov 9, 2017 (structure data deposition date)
AuthorsChen, H.J. / Li, N. / Luo, Y. / Jiang, Y.L. / Zhou, C.Z. / Chen, Y. / Li, Q.
External linksBiochem. J. / PubMed:29555845
MethodsX-ray diffraction
Resolution2.99 Å
Structure data

PDB-5yrp:
Crystal structure of the EAL domain of Mycobacterium smegmatis DcpA
Method: X-RAY DIFFRACTION / Resolution: 2.99 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

Source
  • mycobacterium smegmatis (strain atcc 700084 / mc(2)155) (bacteria)
KeywordsBIOSYNTHETIC PROTEIN / c-di-GMP / diguanylate cyclase / phosphodiesterase / GAF

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