5B0J

Structure of MoeN5-Sso7d fusion protein in complex with beta-undecyl maltoside

Summary for 5B0J

• Entry DOI: 10.2210/pdb5b0j/pdb
• Related: 5B00 5B01 5B02 5B03 5B0I 5B0K 5B0L 5B0M
• Descriptor: MoeN5,DNA-binding protein 7d, UNDECYL-MALTOSIDE (3 entities in total)
• Functional Keywords: prenyltransferase, alpha-helical fold, fusion tag, complex, transferase, dna binding protein
• Biological source: Streptomyces ghanaensis; More
• Total number of polymer chains: 4
• Total formula weight: 151320.30

Authors

Ko, T.-P.,Zhang, L.,Chen, C.-C.,Guo, R.-T.,Oldfield, E.O. (deposition date: 2015-10-30, release date: 2016-03-23, Last modification date: 2023-11-08)

Primary citation

Zhang, L.,Chen, C.C.,Ko, T.P.,Huang, J.W.,Zheng, Y.,Liu, W.,Wang, I.,Malwal, S.R.,Feng, X.,Wang, K.,Huang, C.H.,Hsu, S.T.,Wang, A.H.,Oldfield, E.,Guo, R.T.
Moenomycin Biosynthesis: Structure and Mechanism of Action of the Prenyltransferase MoeN5.
Angew.Chem.Int.Ed.Engl., 55:4716-4720, 2016

PubMed Abstract: The structure of MoeN5, a unique prenyltransferase involved in the biosynthesis of the antibiotic moenomycin, is reported. MoeN5 catalyzes the reaction of geranyl diphosphate (GPP) with the cis-farnesyl group in phosphoglycolipid 5 to form the (C25) moenocinyl-sidechain-containing lipid 7. GPP binds to an allylic site (S1) and aligns well with known S1 inhibitors. Alkyl glycosides, glycolipids, can bind to both S1 and a second site, S2. Long sidechains in S2 are "bent" and co-locate with the homoallylic substrate isopentenyl diphosphate in other prenyltransferases. These observations support a MoeN5 mechanism in which 5 binds to S2 with its C6-C11 group poised to attack C1 in GPP to form the moenocinyl sidechain, with the more distal regions of 5 aligning with the distal glucose in decyl maltoside. The results are of general interest because they provide the first structures of MoeN5 and a structural basis for its mechanism of action, results that will facilitate the design of new antibiotics.

PubMed: 26954060
DOI: 10.1002/anie.201511388

Experimental method

X-RAY DIFFRACTION (2.5 Å)