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-Structure paper
Title | Discovery of a Unique Structural Motif in Lanthipeptide Synthetases for Substrate Binding and Interdomain Interactions. |
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Journal, issue, pages | Angew. Chem. Int. Ed. Engl., Vol. 61, Page e202211382-e202211382, Year 2022 |
Publish date | Jan 5, 2022 (structure data deposition date) |
![]() | Huang, S. / Wang, Y. / Cai, C. / Xiao, X. / Liu, S. / Ma, Y. / Xie, X. / Liang, Y. / Chen, H. / Zhu, J. ...Huang, S. / Wang, Y. / Cai, C. / Xiao, X. / Liu, S. / Ma, Y. / Xie, X. / Liang, Y. / Chen, H. / Zhu, J. / Hegemann, J.D. / Yao, H. / Wei, W. / Wang, H. |
![]() | ![]() ![]() |
Methods | X-ray diffraction |
Resolution | 2.55 Å |
Structure data | ![]() PDB-7wj6: ![]() PDB-7wj7: |
Chemicals | ![]() ChemComp-MG: ![]() ChemComp-HOH: ![]() ChemComp-XYA: |
Source |
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![]() | BIOSYNTHETIC PROTEIN / Lanthipeptide Synthetase / Class III / CurKC / Curvopeptin |