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- PDB-6wo1: Hybrid acetohydroxyacid synthase complex structure with Cryptococ... -
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Basic information
Entry | Database: PDB / ID: 6wo1 | ||||||
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Title | Hybrid acetohydroxyacid synthase complex structure with Cryptococcus neoformans AHAS catalytic subunit and Saccharomyces cerevisiae AHAS regulatory subunit | ||||||
![]() | (Acetohydroxyacid synthase ...) x 2 | ||||||
![]() | TRANSFERASE / AHAS / pyruvate / FAD / dioxygen | ||||||
Function / homology | ![]() acetolactate synthase regulator activity / acetolactate synthase / acetolactate synthase complex / branched-chain amino acid biosynthetic process / acetolactate synthase activity / valine biosynthetic process / isoleucine biosynthetic process / thiamine pyrophosphate binding / mitochondrial nucleoid / enzyme regulator activity ...acetolactate synthase regulator activity / acetolactate synthase / acetolactate synthase complex / branched-chain amino acid biosynthetic process / acetolactate synthase activity / valine biosynthetic process / isoleucine biosynthetic process / thiamine pyrophosphate binding / mitochondrial nucleoid / enzyme regulator activity / flavin adenine dinucleotide binding / magnesium ion binding / mitochondrion Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Guddat, L.W. / Lonhienne, T. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Structures of fungal and plant acetohydroxyacid synthases. Authors: Thierry Lonhienne / Yu Shang Low / Mario D Garcia / Tristan Croll / Yan Gao / Quan Wang / Lou Brillault / Craig M Williams / James A Fraser / Ross P McGeary / Nicholas P West / Michael J ...Authors: Thierry Lonhienne / Yu Shang Low / Mario D Garcia / Tristan Croll / Yan Gao / Quan Wang / Lou Brillault / Craig M Williams / James A Fraser / Ross P McGeary / Nicholas P West / Michael J Landsberg / Zihe Rao / Gerhard Schenk / Luke W Guddat / ![]() ![]() ![]() Abstract: Acetohydroxyacid synthase (AHAS), also known as acetolactate synthase, is a flavin adenine dinucleotide-, thiamine diphosphate- and magnesium-dependent enzyme that catalyses the first step in the ...Acetohydroxyacid synthase (AHAS), also known as acetolactate synthase, is a flavin adenine dinucleotide-, thiamine diphosphate- and magnesium-dependent enzyme that catalyses the first step in the biosynthesis of branched-chain amino acids. It is the target for more than 50 commercial herbicides. AHAS requires both catalytic and regulatory subunits for maximal activity and functionality. Here we describe structures of the hexadecameric AHAS complexes of Saccharomyces cerevisiae and dodecameric AHAS complexes of Arabidopsis thaliana. We found that the regulatory subunits of these AHAS complexes form a core to which the catalytic subunit dimers are attached, adopting the shape of a Maltese cross. The structures show how the catalytic and regulatory subunits communicate with each other to provide a pathway for activation and for feedback inhibition by branched-chain amino acids. We also show that the AHAS complex of Mycobacterium tuberculosis adopts a similar structure, thus demonstrating that the overall AHAS architecture is conserved across kingdoms. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 310.7 KB | Display | ![]() |
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PDB format | ![]() | 249 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.6 MB | Display | ![]() |
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Full document | ![]() | 1.6 MB | Display | |
Data in XML | ![]() | 28.1 KB | Display | |
Data in CIF | ![]() | 37.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6u9dC ![]() 6u9hC ![]() 6vz8C ![]() 2fgcS ![]() 5imsS C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
-Acetohydroxyacid synthase ... , 2 types, 2 molecules AB
#1: Protein | Mass: 78594.672 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Protein | Mass: 34041.734 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Production host: ![]() ![]() |
-Non-polymers , 5 types, 5 molecules ![](data/chem/img/FAD.gif)
![](data/chem/img/8GF.gif)
![](data/chem/img/DPO.gif)
![](data/chem/img/MG.gif)
![](data/chem/img/VAL.gif)
![](data/chem/img/8GF.gif)
![](data/chem/img/DPO.gif)
![](data/chem/img/MG.gif)
![](data/chem/img/VAL.gif)
#3: Chemical | ChemComp-FAD / |
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#4: Chemical | ChemComp-8GF / |
#5: Chemical | ChemComp-DPO / |
#6: Chemical | ChemComp-MG / |
#7: Chemical | ChemComp-VAL / |
-Details
Has ligand of interest | Y |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.77 Å3/Da / Density % sol: 55.62 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / Details: Potassium thiocyanate, PEG 3350 |
-Data collection
Diffraction | Mean temperature: 100 K / Ambient temp details: Oxford cryostream / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 210r / Detector: CCD / Date: Mar 28, 2019 |
Radiation | Monochromator: SI(III) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9537 Å / Relative weight: 1 |
Reflection | Resolution: 3.3→48.92 Å / Num. obs: 19890 / % possible obs: 99.8 % / Redundancy: 19.7 % / Biso Wilson estimate: 92.68 Å2 / CC1/2: 0.999 / Rpim(I) all: 0.041 / Net I/σ(I): 13.7 |
Reflection shell | Resolution: 3.3→3.56 Å / Num. unique obs: 3985 / Rpim(I) all: 0.286 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 5IMS, 2FGC Resolution: 3.3→48.92 Å / SU ML: 0.42 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 26.7
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 253.15 Å2 / Biso mean: 95.6873 Å2 / Biso min: 35.56 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 3.3→48.92 Å
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 14
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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