REL
2024-08-28
2025-02-11
2025-02-11
EcPKS2 with acylated pPANT and three ACP-docked positions
0000-0003-1762-8390
Heidi
Linda
Schubert
Department of Biochemistry; University of Utah
15 N Medical Drive South
Salt Lake City
Utah
United States
84112
0000-0001-6796-7740
Christopher
Hill
University of Utah, Department of Biochemistry
15 N Medical Drive East
Salt Lake City
Utah
United States
84112
Schubert HL
National Science Foundation (NSF, United States)
2203613
United States
2.9
10.6019/EMPIAR-12314
EMDB
molecule
EMD-45913
EMD-45912
EMD-45911
Schubert HL
Li F
Hill CP
Schmidt EW
The structure of full-length AFPK supports the ACP linker in a role that regulates iterative polyketide and fatty acid assembly
Proceedings of the National Academy of Sciences of the United States of America
Proc Natl Acad Sci U S A
United States
6
122
2025
English
10.1073/pnas.2419884122
39913209
The micrographs are EcPKS2 bound to acylated pPANT on the ACP domain and with a acyl-group bound to the b-KetoSynthase domain active site Cys. ACP is docked to the DH domain and partially at the KS domain.
unaligned 40-frame movies, 0.53A/px, 40e/movie
/data
micrographs - multiframe
TIFF
TIFF
6244
40
1
40
UNSIGNED BYTE
11520
1.6
8184
1.6