Structure of 3-oxoacyl-(acyl-carrier protein) synthase II from Thermus thermophilus HB8

The β-ketoacyl-(acyl carrier protein) synthases (β-keto-ACP synthases; KAS) catalyse the addition of two-carbon units to the growing acyl chain during the elongation phase of fatty-acid synthesis. As key regulators of bacterial fatty-acid synthesis, they are promising targets for the development of...

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Main Authors: Bagautdinov, Bagautdin, Ukita, Yoko, Miyano, Masashi, Kunishima, Naoki
Format: Artigo
Sprog:English
Udgivet: International Union of Crystallography 2008
Fag:
Protein Structure Communications
Online adgang:https://ncbi.nlm.nih.gov/pmc/articles/PMC2376401/
https://ncbi.nlm.nih.gov/pubmed/18453702
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S1744309108010336
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spelling pubmed-23764012010-05-01 Structure of 3-oxoacyl-(acyl-carrier protein) synthase II from Thermus thermophilus HB8 Bagautdinov, Bagautdin Ukita, Yoko Miyano, Masashi Kunishima, Naoki Acta Crystallogr Sect F Struct Biol Cryst Commun Protein Structure Communications The β-ketoacyl-(acyl carrier protein) synthases (β-keto-ACP synthases; KAS) catalyse the addition of two-carbon units to the growing acyl chain during the elongation phase of fatty-acid synthesis. As key regulators of bacterial fatty-acid synthesis, they are promising targets for the development of new antibacterial agents. The crystal structure of 3-oxoacyl-ACP synthase II from Thermus thermophilus HB8 (TtKAS II) has been solved by molecular replacement and refined at 2.0 Å resolution. The crystal is orthorhombic, space group P2(1)2(1)2, with unit-cell parameters a = 72.07, b = 185.57, c = 62.52 Å, and contains one homodimer in the asymmetric unit. The subunits adopt the well known α-β-α-β-α thiolase fold that is common to ACP synthases. The structural and sequence similarities of TtKAS II to KAS I and KAS II enzymes of known structure from other sources support the hypothesis of comparable enzymatic activity. The dimeric state of TtKAS II is important to create each fatty-acid-binding pocket. Closer examination of KAS structures reveals that compared with other KAS structures in the apo form, the active site of TtKAS II is more accessible because of the ‘open’ conformation of the Phe396 side chain. International Union of Crystallography 2008-04-30 /pmc/articles/PMC2376401/ /pubmed/18453702 http://dx.doi.org/10.1107/S1744309108010336 Text en © International Union of Crystallography 2008
institution US National Library of Medicine
collection PubMed Central
language English
format Article
topic Protein Structure Communications
spellingShingle Protein Structure Communications
Bagautdinov, Bagautdin
Ukita, Yoko
Miyano, Masashi
Kunishima, Naoki
Structure of 3-oxoacyl-(acyl-carrier protein) synthase II from Thermus thermophilus HB8
description The β-ketoacyl-(acyl carrier protein) synthases (β-keto-ACP synthases; KAS) catalyse the addition of two-carbon units to the growing acyl chain during the elongation phase of fatty-acid synthesis. As key regulators of bacterial fatty-acid synthesis, they are promising targets for the development of new antibacterial agents. The crystal structure of 3-oxoacyl-ACP synthase II from Thermus thermophilus HB8 (TtKAS II) has been solved by molecular replacement and refined at 2.0 Å resolution. The crystal is orthorhombic, space group P2(1)2(1)2, with unit-cell parameters a = 72.07, b = 185.57, c = 62.52 Å, and contains one homodimer in the asymmetric unit. The subunits adopt the well known α-β-α-β-α thiolase fold that is common to ACP synthases. The structural and sequence similarities of TtKAS II to KAS I and KAS II enzymes of known structure from other sources support the hypothesis of comparable enzymatic activity. The dimeric state of TtKAS II is important to create each fatty-acid-binding pocket. Closer examination of KAS structures reveals that compared with other KAS structures in the apo form, the active site of TtKAS II is more accessible because of the ‘open’ conformation of the Phe396 side chain.
author Bagautdinov, Bagautdin
Ukita, Yoko
Miyano, Masashi
Kunishima, Naoki
author_facet Bagautdinov, Bagautdin
Ukita, Yoko
Miyano, Masashi
Kunishima, Naoki
author_sort Bagautdinov, Bagautdin
title Structure of 3-oxoacyl-(acyl-carrier protein) synthase II from Thermus thermophilus HB8
title_short Structure of 3-oxoacyl-(acyl-carrier protein) synthase II from Thermus thermophilus HB8
title_full Structure of 3-oxoacyl-(acyl-carrier protein) synthase II from Thermus thermophilus HB8
title_fullStr Structure of 3-oxoacyl-(acyl-carrier protein) synthase II from Thermus thermophilus HB8
title_full_unstemmed Structure of 3-oxoacyl-(acyl-carrier protein) synthase II from Thermus thermophilus HB8
title_sort structure of 3-oxoacyl-(acyl-carrier protein) synthase ii from thermus thermophilus hb8
publisher International Union of Crystallography
publisher_facet International Union of Crystallography
publishDate 2008
url https://ncbi.nlm.nih.gov/pmc/articles/PMC2376401/
https://ncbi.nlm.nih.gov/pubmed/18453702
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S1744309108010336
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