4GGV

Crystal Structure of HmtT Involved in Himastatin Biosynthesis

Summary for 4GGV

• Entry DOI: 10.2210/pdb4ggv/pdb
• Descriptor: Cytochrome P450 superfamily protein, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• Functional Keywords: cysteine-ligand loop, hydrolase, oxidoreductase
• Biological source: Streptomyces himastatinicus
• Total number of polymer chains: 1
• Total formula weight: 47093.98

Authors

Zhang, H.,Chen, J.,Wang, H.,Zhang, H. (deposition date: 2012-08-07, release date: 2013-07-17, Last modification date: 2023-11-08)

Primary citation

Zhang, H.,Chen, J.,Wang, H.,Xie, Y.,Ju, J.,Yan, Y.,Zhang, H.
Structural analysis of HmtT and HmtN involved in the tailoring steps of himastatin biosynthesis
Febs Lett., 587:1675-1680, 2013

PubMed Abstract: 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.

PubMed: 23611984
DOI: 10.1016/j.febslet.2013.04.013

Experimental method

X-RAY DIFFRACTION (2.331 Å)