5xw2

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

spinqualitylabelsall models 5xw2, resolution 1.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5xw2 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 1.298Å Ligands: GOL, HEM, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function D9WMQ6_9ACTN Publication Abstract from PubMed 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 A), 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. Molecular characterization of the hydroxylase HmtN at 1.3 A resolution.,Zhang H, Chen J, Zhang H Biochem Biophys Res Commun. 2017 Jul 4. pii: S0006-291X(17)31341-4. doi:, 10.1016/j.bbrc.2017.07.010. PMID:28687492 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cytochrome P450 3D structures

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