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Structure paper

TitleEnzyme-catalysed [6+4] cycloadditions in the biosynthesis of natural products.
Journal, issue, pagesNature, Vol. 568, Page 122-126, Year 2019
Publish dateJun 23, 2018 (structure data deposition date)
AuthorsZhang, B. / Wang, K.B. / Wang, W. / Wang, X. / Liu, F. / Zhu, J. / Shi, J. / Li, L.Y. / Han, H. / Xu, K. ...Zhang, B. / Wang, K.B. / Wang, W. / Wang, X. / Liu, F. / Zhu, J. / Shi, J. / Li, L.Y. / Han, H. / Xu, K. / Qiao, H.Y. / Zhang, X. / Jiao, R.H. / Houk, K.N. / Liang, Y. / Tan, R.X. / Ge, H.M.
External linksNature / PubMed:30867595
MethodsX-ray diffraction
Resolution1.618 - 2.3 Å
Structure data

PDB-6a5f:
The structure of [4+2] and [6+4] cyclase in the biosynthetic pathway of nargenicin
Method: X-RAY DIFFRACTION / Resolution: 2.05 Å

PDB-6a5g:
The structure of [4+2] and [6+4] cyclase in the biosynthetic pathway of streptoseomycin
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-6a5h:
The structure of [4+2] and [6+4] cyclase in the biosynthetic pathway of unidentified natural product
Method: X-RAY DIFFRACTION / Resolution: 1.618 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • nocardia argentinensis atcc 31306 (bacteria)
  • streptomyces seoulensis (bacteria)
  • nocardia tenerifensis nbrc 101015 (bacteria)
KeywordsBIOSYNTHETIC PROTEIN / nargenicin / biosynthesis / [4+2] and [4+6] cyclase / Streptoseomycin / natural product

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