6N3P
Crosslinked AcpP=FabZ complex from E. coli Type II FAS
Summary for 6N3P
| Entry DOI | 10.2210/pdb6n3p/pdb |
| Descriptor | 3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ, Acyl carrier protein, N~3~-{(2R)-4-[(dihydroxyphosphanyl)oxy]-2-hydroxy-3,3-dimethylbutanoyl}-N-(3-{[(1Z)-pent-1-en-1-yl]sulfonyl}propyl)-beta-alaninamide, ... (4 entities in total) |
| Functional Keywords | fatty acid biosynthsis, fas, dehydratase, crosslinking, acyl carrier protein, acp, fabz, acpp, e. coli, biosynthetic protein |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 12 |
| Total formula weight | 159421.26 |
| Authors | Smith, J.L.,Dodge, G.J. (deposition date: 2018-11-15, release date: 2019-03-13, Last modification date: 2024-10-23) |
| Primary citation | Dodge, G.J.,Patel, A.,Jaremko, K.L.,McCammon, J.A.,Smith, J.L.,Burkart, M.D. Structural and dynamical rationale for fatty acid unsaturation inEscherichia coli. Proc. Natl. Acad. Sci. U.S.A., 116:6775-6783, 2019 Cited by PubMed Abstract: Fatty acid biosynthesis in α- and γ-proteobacteria requires two functionally distinct dehydratases, FabA and FabZ. Here, mechanistic cross-linking facilitates the structural characterization of a stable hexameric complex of six FabZ dehydratase subunits with six AcpP acyl carrier proteins. The crystal structure sheds light on the divergent substrate selectivity of FabA and FabZ by revealing distinct architectures of the binding pocket. Molecular dynamics simulations demonstrate differential biasing of substrate orientations and conformations within the active sites of FabA and FabZ such that FabZ is preorganized to catalyze only dehydration, while FabA is primed for both dehydration and isomerization. PubMed: 30872475DOI: 10.1073/pnas.1818686116 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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