4WV3

Crystal structure of the anthranilate CoA ligase AuaEII in complex with anthranoyl-AMP

Summary for 4WV3

• Entry DOI: 10.2210/pdb4wv3/pdb
• Descriptor: Anthranilate-CoA ligase, 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine (3 entities in total)
• Functional Keywords: anthranilate, coa ligase, aurachin, natural product biosynthesis, ligase-ligase inhibitor complex, ligase/ligase inhibitor
• Biological source: Stigmatella aurantiaca
• Total number of polymer chains: 2
• Total formula weight: 118284.35

Authors

Tsai, S.C.,Muller, R.,Jackson, D.R.,Tu, S.S.,Nguyen, M.,Barajas, J.F.,Pistorious, D.,Krug, D. (deposition date: 2014-11-04, release date: 2015-11-11, Last modification date: 2023-09-27)

Primary citation

Jackson, D.R.,Tu, S.S.,Nguyen, M.,Barajas, J.F.,Schaub, A.J.,Krug, D.,Pistorius, D.,Luo, R.,Muller, R.,Tsai, S.C.
Structural Insights into Anthranilate Priming during Type II Polyketide Biosynthesis.
Acs Chem.Biol., 11:95-103, 2016

PubMed Abstract: The incorporation of nonacetate starter units during type II polyketide biosynthesis helps diversify natural products. Currently, there are few enzymatic strategies for the incorporation of nonacetate starter units in type II polyketide synthase (PKS) pathways. Here we report the crystal structure of AuaEII, the anthranilate:CoA ligase responsible for the generation of anthraniloyl-CoA, which is used as a starter unit by a type II PKS in aurachin biosynthesis. We present structural and protein sequence comparisons to other aryl:CoA ligases. We also compare the AuaEII crystal structure to a model of a CoA ligase homologue, AuaE, which is present in the same gene cluster. AuaE is predicted to have the same fold as AuaEII, but instead of CoA ligation, AuaE catalyzes acyl transfer of anthranilate from anthraniloyl-CoA to the acyl carrier protein (ACP). Together, this work provides insight into the molecular basis for starter unit selection of anthranilate in type II PKS biosynthesis.

PubMed: 26473393
DOI: 10.1021/acschembio.5b00500

Experimental method

X-RAY DIFFRACTION (2.599 Å)