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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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