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. 2019 Sep 1;75(Pt 9):570-575.
doi: 10.1107/S2053230X19010914. Epub 2019 Aug 28.

Crystal structure of TchmY from Actinoplanes teichomyceticus

Zhenzhen Yang  1 , Lilan Zhang  2 , Xuejing Yu  2 , Shan Wu  2 , Yong Yang  2 , Yumei Hu  2 , Qian Li  3 , Na Shang  3 , Rey Ting Guo  2 , Chun Chi Chen  2 , Longhai Dai  2 , Weidong Liu  1
Affiliations

Crystal structure of TchmY from Actinoplanes teichomyceticus

Zhenzhen Yang et al. Acta Crystallogr F Struct Biol Commun. .

Abstract

Moenomycin-type antibiotics are phosphoglycolipids that are notable for their unique modes of action and have proven to be useful in animal nutrition. The gene clusters tchm from Actinoplanes teichomyceticus and moe from Streptomyces are among a limited number of known moenomycin-biosynthetic pathways. Most genes in tchm have counterparts in the moe cluster, except for tchmy and tchmz, the functions of which remain unknown. Sequence analysis indicates that TchmY belongs to the isoprenoid enzyme C2-like superfamily and may serve as a prenylcyclase. The enzyme was proposed to be involved in terminal cyclization of the moenocinyl chain in teichomycin, leading to the diumycinol chain of moenomycin isomers. Here, recombinant TchmY protein was expressed in Escherichia coli and its crystal structure was solved by SIRAS. Structural analysis and comparison with other prenylcyclases were performed. The overall fold of TchmY consists of an (α/α)6-barrel, and a potential substrate-binding pocket is found in the central chamber. These results should provide important information regarding the biosynthetic basis of moenomycin antibiotics.

Keywords: Actinoplanes teichomyceticus; crystal structure; prenylcyclases.

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Figures

Figure 1
Figure 1
Structures of moenomycins.
Figure 2
Figure 2
Picture of a crystal of TchmY.
Figure 3
Figure 3
Overall structure of TchmY. A cartoon model of TchmY is depicted and displayed in different orientations. Individual helices are labeled. The outer and inner shells of the (α/α)6-barrel are shown in pink and cyan, respectively. The bound ligands are shown as yellow sticks.
Figure 4
Figure 4
Structural comparison of TchmY and two terpene cyclases. Cartoon models of TchmY (green), HsOSC (cyan; PDB entry 1w6k) and PtmT2 (magenta; PDB entry 5bp8) are depicted: top and side views are displayed. The substrate-binding site of HsOSC is indicated and the bound substrate is presented in stick representation. The domain arrangements of HsOSC and PtmT2 are indicated by dashed boxes.
Figure 5
Figure 5
Structural comparison of TchmY and similar (α/α)6-barrel proteins. (a, b) Alignment of TchmY (green) and bovine transcobalamin (yellow; PDB entry 2bb6); (c, d) alignment of TchmY (green) and cellobiose 2-epimerase (purple; PDB entry 3wkg); (e, f) alignment of TchmY (green) and geranylgeranyltransferase (blue; PDB entry 3dra). The substrates of the three structures are presented in stick representation and are shown in pink for clarity.
See this image and copyright information in PMC

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