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Structure paper

TitleStructural and functional analysis of two di-domain aromatase/cyclases from type II polyketide synthases.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 112, Page E6844-E6851, Year 2015
Publish dateJan 21, 2015 (structure data deposition date)
AuthorsCaldara-Festin, G. / Jackson, D.R. / Barajas, J.F. / Valentic, T.R. / Patel, A.B. / Aguilar, S. / Nguyen, M. / Vo, M. / Khanna, A. / Sasaki, E. ...Caldara-Festin, G. / Jackson, D.R. / Barajas, J.F. / Valentic, T.R. / Patel, A.B. / Aguilar, S. / Nguyen, M. / Vo, M. / Khanna, A. / Sasaki, E. / Liu, H.W. / Tsai, S.C.
External linksProc. Natl. Acad. Sci. USA / PubMed:26631750
MethodsX-ray diffraction
Resolution1.79 - 1.952 Å
Structure data

PDB-4xrt:
Crystal structure of the di-domain ARO/CYC StfQ from the steffimycin biosynthetic pathway
Method: X-RAY DIFFRACTION / Resolution: 1.952 Å

PDB-4xrw:
Crystal structure of the di-domain ARO/CYC BexL from the BE-7585A biosynthetic pathway
Method: X-RAY DIFFRACTION / Resolution: 1.79 Å

Chemicals

ChemComp-FMT:
FORMIC ACID

ChemComp-HOH:
WATER

ChemComp-MES:
2-(N-MORPHOLINO)-ETHANESULFONIC ACID / pH buffer*YM

Source
  • streptomyces steffisburgensis (bacteria)
  • amycolatopsis orientalis (bacteria)
KeywordsLYASE / aromatase/cyclase / helix-grip fold / polyketide / polyketide synthase / natural products / dehydratase / ARO/CYC

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