5XW2

Crystal structure of the Hydroxylase HmtN in C 1 2 1 crystal form

Summary for 5XW2

• Entry DOI: 10.2210/pdb5xw2/pdb
• Related: 4E2P
• Descriptor: Cytochrome P450 107B1 (P450CVIIB1), PROTOPORPHYRIN IX CONTAINING FE, GLYCEROL, ... (5 entities in total)
• Functional Keywords: himastatin, hydroxylase, cytochrome p450, biosynthetic protein
• Biological source: Streptomyces himastatinicus ATCC 53653
• Total number of polymer chains: 1
• Total formula weight: 48026.65

Authors

Zhang, H.D.,Zhang, H.J. (deposition date: 2017-06-29, release date: 2018-04-25, Last modification date: 2023-11-22)

Primary citation

Zhang, H.,Chen, J.,Zhang, H.
Molecular characterization of the hydroxylase HmtN at 1.3 angstrom resolution.
Biochem. Biophys. Res. Commun., 2017

PubMed Abstract: Himastatin is a novel antibiotic with antitumor and antibacterial activity. In the himastatin biosynthesis pathway, HmtN is responsible for the hydroxylation of the piperazic acid (Pip) motif. Herein, we present the crystal structures of HmtN (1.3 Å), which is the first structure for a cytochrome P450 involved in the hydroxylation of cyclohexadepsipeptide during himastatin biosynthesis. Structure analysis indicated that almost all the surface of HmtN has negative electrostatic potential, only small patches of positive electrostatic potential can be found. It is worth noting that almost the entire active site of HmtT is negatively charged, while HmtN active site is composed of positive and negative charge. This may be relevant to their specific substrate recognition and different catalytic function. In addition, three channels were observed in HmtN crystal structure; channel 3 may be essential for substrate ingress and egress from the active site to the surface, while channel 1 and channel 2 may be the solvent and water pathway, respectively.

PubMed: 28687492
DOI: 10.1016/j.bbrc.2017.07.010

Experimental method

X-RAY DIFFRACTION (1.298 Å)