6J8W

Structure of MOEN5-SSO7D fusion protein in complex with lig 1

Summary for 6J8W

• Entry DOI: 10.2210/pdb6j8w/pdb
• Related: 5gwv
• Descriptor: MoeN5,DNA-binding protein 7d, (2S)-3-dimethoxyphosphoryloxy-2-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trienoxy]propanoic acid (3 entities in total)
• Functional Keywords: moenomycin, antibiotics, biosynthesis, prenyl transferase, alpha, transferase
• Biological source: Streptomyces ghanaensis; More
• Total number of polymer chains: 4
• Total formula weight: 151164.05

Authors

Ko, T.P.,Zhang, L.L.,Chen, C.C.,Guo, R.T. (deposition date: 2019-01-21, release date: 2019-04-17, Last modification date: 2023-11-22)

Primary citation

Zhang, L.L.,Ko, T.P.,Malwal, S.R.,Liu, W.D.,Zhou, S.Y.,Yu, X.J.,Oldfield, E.,Guo, R.T.,Chen, C.C.
Complex structures of MoeN5 with substrate analogues suggest sequential catalytic mechanism.
Biochem. Biophys. Res. Commun., 511:800-805, 2019

PubMed Abstract: The antibiotic moenomycin A is a phosphoglycerate derivative with a C-moenocinyl chain and a branched oligosaccharide. Formation of the C-chain is catalyzed by the enzyme MoeN5 with geranyl pyrophosphate (GPP) and the sugar-linked 2-Z,E-farnesyl-3-phosphoglycerate (FPG) as its substrates. Previous complex crystal structures with GPP and long-chain alkyl glycosides suggested that GPP binds to the S1 site in a similar way as in most other α-helical prenyltransferases (PTs), and FPG is likely to assume a bent conformation in the S2 site. However, two FPG derivatives synthesized in the current study were found in the S1 site rather than S2 in their complex crystal structures with MoeN5. Apparently S1 is the preferred site for prenyl-containing ligand, and S2 binding may proceed only after S1 is occupied. Thus, like most trans-type PTs, MoeN5 may employ a sequential ionization-condensation-elimination mechanism that involves a carbocation intermediate.

PubMed: 30837154
DOI: 10.1016/j.bbrc.2019.02.131

Experimental method

X-RAY DIFFRACTION (2.35 Å)