Structural basis for different membrane-binding properties of<i> E.</i><i> coli</i> anaerobic and human mitochondrial 8-oxidation trifunctional enzymes

SAH-TELI, Shiv K, Matyáš PINKAS, Mikko J HYNONEN, Sarah J BUTCHER, Rik K WIERENGA, Jiří NOVÁČEK and Rajaram VENKATESAN. Structural basis for different membrane-binding properties of<i> E.</i><i> coli</i> anaerobic and human mitochondrial 8-oxidation trifunctional enzymes. Structure. CAMBRIDGE: CELL PRESS, 2023, vol. 31, No 7, p. 812-832. ISSN 0969-2126. Available from: https://dx.doi.org/10.1016/j.str.2023.04.011.

Basic information

• Original name: Structural basis for different membrane-binding properties of<i> E.</i><i> coli</i> anaerobic and human mitochondrial 8-oxidation trifunctional enzymes
• Authors: SAH-TELI, Shiv K, Matyáš PINKAS (203 Czech Republic, belonging to the institution), Mikko J HYNONEN, Sarah J BUTCHER, Rik K WIERENGA, Jiří NOVÁČEK (203 Czech Republic, belonging to the institution) and Rajaram VENKATESAN (guarantor).
• Edition: Structure, CAMBRIDGE, CELL PRESS, 2023, 0969-2126.

Other information

• Original language: English
• Type of outcome: Article in a journal
• Field of Study: 10608 Biochemistry and molecular biology
• Country of publisher: United States of America
• Confidentiality degree: is not subject to a state or trade secret
• WWW: URL
• Impact factor: Impact factor: 5.700 in 2022
• RIV identification code: RIV/00216224:14740/23:00133567
• Organization unit: Central European Institute of Technology
• Doi: http://dx.doi.org/10.1016/j.str.2023.04.011
• UT WoS: 001041738700001
• Keywords in English: ACID BETA-OXIDATION; MULTIENZYME COMPLEX; CRYSTAL-STRUCTURE; ESCHERICHIA-COLI; MULTIFUNCTIONAL ENZYME; FATTY-ACIDS; INTERMEDIATE; RESOLUTION; BIOSYNTHESIS; REVERSAL
• Tags: CF CRYO, rivok
• Tags: International impact, Reviewed

Abstract

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.

Links

• EF18_046/0015974, research and development project: Name: Modernizace České infrastruktury pro integrativní strukturní biologii
• LM2023042, research and development project: Name: Česká infrastruktura pro integrativní strukturní biologii

Investor: Ministry of Education, Youth and Sports of the CR, CIISB - Czech Infrastructure for Integrative Structural Biology

• 653706, interní kód MU: Name: iNEXT - Infrastructure for NMR, EM and X-ray crystallography for translational research (Acronym: iNEXT)

Investor: European Union, iNEXT - Infrastructure for NMR, EM and X-ray crystallography for translational research, RI Research Infrastructures (Excellent Science)

• 871037, interní kód MU: Name: iNEXT-Discovery: Infrastructure for transnational access and discovery in integrated structural biology (Acronym: iNEXT- Discovery)

Investor: European Union, RI Research Infrastructures (Excellent Science)

• 90242, large research infrastructures: Name: CIISB III