Journal
FEBS LETTERS
Volume 587, Issue 11, Pages 1675-1680Publisher
WILEY
DOI: 10.1016/j.febslet.2013.04.013
Keywords
Himastatin; HmtT; HmtN; Cytochrome P450; Crystal structure
Funding
- National Natural Science Foundation of China [31000326, 20872152]
- National Key Basic Research Program of China [2013CB933900]
- Fundamental Research Funds for the Central Universities [01-18170005]
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Himastatin is a novel antibiotic featuring a bicyclohexadepsipeptide structure. On the himastatin biosynthesis pathway, three cytochrome P450s (HmtT, HmtN, HmtS) are responsible for the post-tailoring of the cyclohexadepsipeptide backbone. Here we report the crystal structures of HmtT and HmtN. The overall structures of these two proteins are homologous to other cytochrome P450s. However, the exceptionally long F-G loop in HmtT has a highly unusual conformation and extends deep into the active site. As a result, the F/G helices of HmtT are both kinked. In contrast, the F/G helices of HmtN are straight. Also, the F/G helices in HmtT and HmtN take distinctive orientations, which may be a contributing factor for the substrate specificity of these two enzymes. (c) 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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