5H1Z

CYP153D17 from Sphingomonas sp. PAMC 26605

Summary for 5H1Z

• Entry DOI: 10.2210/pdb5h1z/pdb
• Descriptor: putative CYP alkane hydroxylase CYP153D17, PROTOPORPHYRIN IX CONTAINING FE, DODECANE, ... (4 entities in total)
• Functional Keywords: p450, alkane hydroxylase, cyp153d17, sphingomonas sp. pamc 26605, hydrolase
• Biological source: Sphingomonas sp. PAMC 26605
• Total number of polymer chains: 1
• Total formula weight: 47612.20

Authors

Lee, C.W.,Lee, J.H. (deposition date: 2016-10-13, release date: 2017-01-11, Last modification date: 2024-03-20)

Primary citation

Lee, C.W.,Yu, S.C.,Lee, J.H.,Park, S.H.,Park, H.,Oh, T.J.,Lee, J.H.
Crystal Structure of a Putative Cytochrome P450 Alkane Hydroxylase (CYP153D17) from Sphingomonas sp. PAMC 26605 and Its Conformational Substrate Binding
Int J Mol Sci, 17:-, 2016

PubMed Abstract: Enzymatic alkane hydroxylation reactions are useful for producing pharmaceutical and agricultural chemical intermediates from hydrocarbons. Several cytochrome P450 enzymes catalyze the regio- and stereo-specific hydroxylation of alkanes. We evaluated the substrate binding of a putative CYP alkane hydroxylase (CYP153D17) from the bacterium sp. PAMC 26605. Substrate affinities to C10-C12 n-alkanes and C10-C14 fatty acids with values varied from 0.42 to 0.59 μM. A longer alkane (C12) bound more strongly than a shorter alkane (C10), while shorter fatty acids (C10, capric acid; C12, lauric acid) bound more strongly than a longer fatty acid (C14, myristic acid). These data displayed a broad substrate specificity of CYP153D17, hence it was named as a putative CYP alkane hydroxylase. Moreover, the crystal structure of CYP153D17 was determined at 3.1 Å resolution. This is the first study to provide structural information for the CYP153D family. Structural analysis showed that a co-purified alkane-like compound bound near the active-site heme group. The alkane-like substrate is in the hydrophobic pocket containing Thr74, Met90, Ala175, Ile240, Leu241, Val244, Leu292, Met295, and Phe393. Comparison with other CYP structures suggested that conformational changes in the β1-β2, α3-α4, and α6-α7 connecting loop are important for incorporating the long hydrophobic alkane-like substrate. These results improve the understanding of the catalytic mechanism of CYP153D17 and provide valuable information for future protein engineering studies.

PubMed: 27941697
DOI: 10.3390/ijms17122067

Experimental method

X-RAY DIFFRACTION (3.1 Å)