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Structure of MOEN5-SSO7D fusion protein in complex with lig 1
Structural highlights
FunctionA0A010_STRVD DN7D_SACS2 Can constrain negative DNA supercoils. May be involved in maintaining the integrity of the genome at high temperature (By similarity). Stimulates the Holliday junction cleavage activity of Hjc (PubMed:11709558).[UniProtKB:P61990][1] Publication Abstract from PubMedThe antibiotic moenomycin A is a phosphoglycerate derivative with a C25-moenocinyl chain and a branched oligosaccharide. Formation of the C25-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 alpha-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. Complex structures of MoeN5 with substrate analogues suggest sequential catalytic mechanism.,Zhang L, Ko TP, Malwal SR, Liu W, Zhou S, Yu X, Oldfield E, Guo RT, Chen CC Biochem Biophys Res Commun. 2019 Apr 16;511(4):800-805. doi:, 10.1016/j.bbrc.2019.02.131. Epub 2019 Mar 2. PMID:30837154[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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