Structural insights into the binding of lauric acid to CYP107L2 from Streptomyces avermitilis

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• 作者：Songhee Han^a ; Tan-Viet Pham^a ; ^d ; Joo-Hwan Kim^a ; Young-Ran Lim^a ; Hyoung-Goo Park^a ; Dabin Jeong^a ; Chul-Ho Yun^b ; Young-Jin Chun^c ; Lin-Woo Kang^a ; ^{lkang@konkuk.ac.kr} ; Donghak Kim^a ; ^{donghak@konkuk.ac.kr}
• 关键词：P450 ; CYP ; CYP107L2 ; Streptomyces avermitilis ; Lauric acid ; X-ray crystal structure
• 刊名：Biochemical and Biophysical Research Communications
• 出版年：2017
• 出版时间：22 January 2017
• 年：2017
• 卷：482
• 期：4
• 页码：902-908
• 全文大小：1346 K
• 卷排序：482

文摘

CYP107L2 from S. avermitilis shares a high sequence similarity with the PikC. Purified CYP107L2 yielded a typical type I binding spectra to pikromycin and lauric acid. Crystal structure of CYP107L2 complex with lauric acid was determined at 2.5 Å resolution. Laurate is bound mainly via hydrophobic interactions in the substrate binding cavity of CYP107L2.