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@article{2375377, author = {SahandTeli, Shiv K and Pinkas, Matyáš and Hynonen, Mikko J and Butcher, Sarah J and Wierenga, Rik K and Nováček, Jiří and Venkatesan, Rajaram}, article_location = {CAMBRIDGE}, article_number = {7}, doi = {http://dx.doi.org/10.1016/j.str.2023.04.011}, keywords = {ACID BETA-OXIDATION; MULTIENZYME COMPLEX; CRYSTAL-STRUCTURE; ESCHERICHIA-COLI; MULTIFUNCTIONAL ENZYME; FATTY-ACIDS; INTERMEDIATE; RESOLUTION; BIOSYNTHESIS; REVERSAL}, language = {eng}, issn = {0969-2126}, journal = {Structure}, title = {Structural basis for different membrane-binding properties of<i> E.</i><i> coli</i> anaerobic and human mitochondrial 8-oxidation trifunctional enzymes}, url = {https://www.sciencedirect.com/science/article/pii/S096921262300134X?via%3Dihub}, volume = {31}, year = {2023} }
TY - JOUR ID - 2375377 AU - Sah-Teli, Shiv K - Pinkas, Matyáš - Hynonen, Mikko J - Butcher, Sarah J - Wierenga, Rik K - Nováček, Jiří - Venkatesan, Rajaram PY - 2023 TI - Structural basis for different membrane-binding properties of<i> E.</i><i> coli</i> anaerobic and human mitochondrial 8-oxidation trifunctional enzymes JF - Structure VL - 31 IS - 7 SP - 812-832 EP - 812-832 PB - CELL PRESS SN - 09692126 KW - ACID BETA-OXIDATION KW - MULTIENZYME COMPLEX KW - CRYSTAL-STRUCTURE KW - ESCHERICHIA-COLI KW - MULTIFUNCTIONAL ENZYME KW - FATTY-ACIDS KW - INTERMEDIATE KW - RESOLUTION KW - BIOSYNTHESIS KW - REVERSAL UR - https://www.sciencedirect.com/science/article/pii/S096921262300134X?via%3Dihub N2 - Facultative anaerobic bacteria such as Escherichia coli have two a282 heterotetrameric trifunctional en-zymes (TFE), catalyzing the last three steps of the 8-oxidation cycle: soluble aerobic TFE (EcTFE) and membrane-associated anaerobic TFE (anEcTFE), closely related to the human mitochondrial TFE (HsTFE). The cryo-EM structure of anEcTFE and crystal structures of anEcTFE-a show that the overall assembly of anEcTFE and HsTFE is similar. However, their membrane-binding properties differ consider-ably. The shorter A5-H7 and H8 regions of anEcTFE-a result in weaker a-8 as well as a-membrane interactions, respectively. The protruding H-H region of anEcTFE-8 is therefore more critical for membrane-association. Mutational studies also show that this region is important for the stability of the anEcTFE-8 dimer and anEcTFE heterotetramer. The fatty acyl tail binding tunnel of the anEcTFE-a hydra-tase domain, as in HsTFE-a, is wider than in EcTFE-a, accommodating longer fatty acyl tails, in good agreement with their respective substrate specificities. ER -
SAH-TELI, Shiv K, Matyáš PINKAS, Mikko J HYNONEN, Sarah J BUTCHER, Rik K WIERENGA, Jiří NOVÁČEK a Rajaram VENKATESAN. Structural basis for different membrane-binding properties of\&{}lt;i\&{}gt; E.\&{}lt;/i\&{}gt;\&{}lt;i\&{}gt; coli\&{}lt;/i\&{}gt; anaerobic and human mitochondrial 8-oxidation trifunctional enzymes. \textit{Structure}. CAMBRIDGE: CELL PRESS, 2023, roč.~31, č.~7, s.~812-832. ISSN~0969-2126. Dostupné z: https://dx.doi.org/10.1016/j.str.2023.04.011.
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