5it1

Streptomyces peucetius CYP105P2 complex with biphenyl compound

spinqualitylabelsall models 5it1, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5it1 is a 4 chain structure with sequence from Streptomyces peucetius. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Ligands: 2OH, HEM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q70AS3_STRPE Publication Abstract from PubMed Cytochrome P450 monooxygenases (CYP, EC 1.14.14.1) belong to a large family of enzymes that catalyze the hydroxylation of various substrates. Here, we present the crystal structure of CYP105P2 isolated from Streptomyces peucetius ATCC27952 at a 2.1 A resolution. The structure shows the presence of a pseudo-ligand molecule in the active site, which was co-purified fortuitously and is presumed to be a biphenyl derivative. Comparison with previously determined substrate-bound CYP structures showed that binding of the ligand produces large and distinctive conformational changes in alpha2-alpha3, alpha7-alpha9, and the C-terminal loop regions. This structural flexibility confirms our previous observation that CYP105P2 can accommodate a broad range of ligands. The structure complexed with a pseudo-ligand provides the first molecular view of CYP105P2-ligand interactions, and it indicates the involvement of hydrophobic residues (Pro82, Ala181, Met187, Leu189, Leu193, and Ile236) in the interactions between hydrophobic ligands and CYP105P2. These results provide useful insights into the structural changes involved in the recognition of different ligands by CYP105P2. Crystal Structure of Cytochrome P450 (CYP105P2) from Streptomyces peucetius and Its Conformational Changes in Response to Substrate Binding.,Lee CW, Lee JH, Rimal H, Park H, Lee JH, Oh TJ Int J Mol Sci. 2016 May 25;17(6). pii: E813. doi: 10.3390/ijms17060813. PMID:27231902 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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