Involvement of subdomain II in the recognition of acetyl‐CoA revealed by the crystal structure of homocitrate synthase from Sulfolobus acidocaldarius

FEBS Journal ◽  
2020 ◽  
Author(s):  
Tomohiro Suzuki ◽  
Takeo Tomita ◽  
Kenta Hirayama ◽  
Michio Suzuki ◽  
Tomohisa Kuzuyama ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Sulfolobus Acidocaldarius ◽  
Acetyl Coa ◽  
Homocitrate Synthase

scholarly journals X-ray crystal structure of a malonate-semialdehyde dehydrogenase fromPseudomonassp. strain AAC

2017 ◽  
Vol 73 (1) ◽  
pp. 24-28 ◽  
Author(s):  
Matthew Wilding ◽  
Colin Scott ◽  
Thomas S. Peat ◽  
Janet Newman
Keyword(s):  
Crystal Structure ◽  
Search Model ◽  
Molecular Replacement ◽  
X Rays ◽  
X Ray Diffraction ◽  
Acetyl Coa ◽  
Space Group ◽  
X Ray ◽  
Semialdehyde Dehydrogenase

The NAD-dependent malonate-semialdehyde dehydrogenase KES23460 fromPseudomonassp. strain AAC makes up half of a bicistronic operon responsible for β-alanine catabolism to produce acetyl-CoA. The KES23460 protein has been heterologously expressed, purified and used to generate crystals suitable for X-ray diffraction studies. The crystals belonged to space groupP212121and diffracted X-rays to beyond 3 Å resolution using the microfocus beamline of the Australian Synchrotron. The structure was solved using molecular replacement, with a monomer from PDB entry 4zz7 as the search model.

Crystal structure of an Lrs14-like archaeal biofilm regulator fromSulfolobus acidocaldarius

2018 ◽  
Vol 74 (11) ◽  
pp. 1105-1114
Author(s):  
Marian S. Vogt ◽  
Simon L. Völpel ◽  
Sonja-Verena Albers ◽  
Lars-Oliver Essen ◽  
Ankan Banerjee
Keyword(s):  
Crystal Structure ◽  
Biofilm Formation ◽  
Coiled Coil ◽  
Transcriptional Regulators ◽  
Bioinformatic Analysis ◽  
Considerable Degree ◽  
Sulfolobus Acidocaldarius ◽  
Asymmetric Unit ◽  
Winged Helix ◽  
Structural Differences

The small winged helix–turn–helix (wHTH) proteins of the Lrs14 family are major transcriptional regulators and act as archaeal biofilm regulators (AbfRs) in the crenarchaeoteSulfolobus acidocaldarius. Here, the first crystal structure of an AbfR ortholog, AbfR2, the deletion of which is known to impair biofilm formation, is presented. Like most other wHTH orthologs, AbfR2 is dimeric in solution as well as in its 2.45 Å resolution crystal structure. Given the presence of three independent AbfR2 dimers in the asymmetric unit, the crystal structure shows a considerable degree of conformational variation within the dimer, the antiparallel orientations of which are stabilized by coiled-coil interaction between H4 helices. Conserved anchor interactions between helices H0 and H4 of AbfR2 further contribute to dimer stabilization. The combined structural and bioinformatic analysis reveals cluster-specific structural differences between different members of the Lrs14 protein family.

scholarly journals Crystal structure of the β-subunit of acetyl-CoA carboxylase inC. glutamicum

2005 ◽  
Vol 61 (a1) ◽  
pp. c189-c189
Author(s):  
R. Natsume ◽  
M. Yamada ◽  
M. Senda ◽  
T. Nakamatsu ◽  
S. Horinouchi ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Β Subunit ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa

The 1.75 Å Crystal Structure of Acetyl-CoA Synthetase Bound to Adenosine-5‘-propylphosphate and Coenzyme A†

Biochemistry ◽  
2003 ◽  
Vol 42 (10) ◽  
pp. 2866-2873 ◽  
Author(s):  
Andrew M. Gulick ◽  
Vincent J. Starai ◽  
Alexander R. Horswill ◽  
Kristen M. Homick ◽  
Jorge C. Escalante-Semerena
Keyword(s):  
Crystal Structure ◽  
Coenzyme A ◽  
Acetyl Coa

Crystal structure of an acetyl-CoA acetyltransferase from PHB producing bacterium Bacillus cereus ATCC 14579

2020 ◽  
Vol 533 (3) ◽  
pp. 442-448
Author(s):  
Jiyeon Hong ◽  
Woojin Park ◽  
Hogyun Seo ◽  
Il-Kwon Kim ◽  
Kyung-Jin Kim
Keyword(s):  
Crystal Structure ◽  
Bacillus Cereus ◽  
Acetyl Coa ◽  
Bacterium Bacillus

scholarly journals Crystal structure of the 500-kDa yeast acetyl-CoA carboxylase holoenzyme dimer

Nature ◽  
2015 ◽  
Vol 526 (7575) ◽  
pp. 723-727 ◽  
Author(s):  
Jia Wei ◽  
Liang Tong
Keyword(s):  
Crystal Structure ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa

scholarly journals Correction to Novel Domain Arrangement in the Crystal Structure of a Truncated Acetyl-CoA Synthase fromMoorella thermoacetica

Biochemistry ◽  
2009 ◽  
Vol 48 (50) ◽  
pp. 12058-12058 ◽  
Author(s):  
Anne Volbeda ◽  
Claudine Darnault ◽  
Xiangshi Tan ◽  
Paul A. Lindahl ◽  
Juan C. Fontecilla-Camps
Keyword(s):  
Crystal Structure ◽  
Acetyl Coa ◽  
Domain Arrangement

Refined crystal structure of a superoxide dismutase from the hyperthermophilic archaeon Sulfolobus acidocaldarius at 2.2 Å resolution 1 1Edited by R. Huber

1999 ◽  
Vol 285 (2) ◽  
pp. 689-702 ◽  
Author(s):  
Stefan Knapp ◽  
Simone Kardinahl ◽  
Niklas Hellgren ◽  
Gudrun Tibbelin ◽  
Günter Schäfer ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Superoxide Dismutase ◽  
Sulfolobus Acidocaldarius ◽  
Hyperthermophilic Archaeon

Biosynthesis of lysine in Saccharomyces cerevisiae: properties and spectrophotometric determination of homocitrate synthase activity

1976 ◽  
Vol 22 (11) ◽  
pp. 1664-1667 ◽  
Author(s):  
Gary S. Gray ◽  
J. K. Bhattacharjee
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Biosynthetic Pathway ◽  
Wild Type Strain ◽  
Wild Type ◽  
Temperature Optimum ◽  
Acetyl Coa ◽  
Metal Chelating ◽  
Binding Agents ◽  
Homocitrate Synthase

A rapid assay is described for homocitrate synthase (EC 4.1.3.21) of the lysine biosynthetic pathway of Saccharomyces cerevisiae. The α-ketoglutarate-dependent cleavage of acetyl-coA was measured spectrophotometrically as decrease in absorbance at 600 nm in the presence of 2, 6-dichlorophenol-indophenol and enzyme from the wild-type strain X2180. This activity was also present in a citrate synthaseless glutamate auxotroph glu3, and the activity was inhibited by 5 mML-lysine. Radioactive homocitric acid was obtained from a reaction mixture containing [1-14C]acetyl-coA. Homocitrate synthase activity was dependent upon time, both substrates, and enzyme. The activity exhibited a pH and temperature optimum of 7.5–8.0 and 32 °C, respectively, and was inhibited by metal-chelating and sulfhydryl-binding agents.

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