4ggv

Crystal Structure of HmtT Involved in Himastatin Biosynthesis

spinqualitylabelsall models 4ggv, resolution 2.33Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ggv is a 1 chain structure with sequence from Streptomyces himastatinicus ATCC 53653. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.331Å Ligands: HEM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function D9WMR2_9ACTN Publication Abstract from PubMed 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. Structural analysis of HmtT and HmtN involved in the tailoring steps of himastatin biosynthesis.,Zhang H, Chen J, Wang H, Xie Y, Ju J, Yan Y, Zhang H FEBS Lett. 2013 Jun 5;587(11):1675-80. doi: 10.1016/j.febslet.2013.04.013. Epub, 2013 Apr 20. PMID:23611984 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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