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Structure paper

TitleStructures of fungal and plant acetohydroxyacid synthases.
Journal, issue, pagesNature, Vol. 586, Issue 7828, Page 317-321, Year 2020
Publish dateJul 8, 2020
AuthorsThierry 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 /
PubMed AbstractAcetohydroxyacid 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.
External linksNature / PubMed:32640464
MethodsEM (single particle) / X-ray diffraction
Resolution3.194 - 3.8 Å
Structure data

20700

6u9h

EMDB-20700, PDB-6u9h:
Arabidopsis thaliana acetohydroxyacid synthase complex
Method: EM (single particle) / Resolution: 3.8 Å

21487

6vz8

EMDB-21487, PDB-6vz8:
Arabidopsis thaliana acetohydroxyacid synthase complex with valine bound
Method: EM (single particle) / Resolution: 3.45 Å

PDB-6u9d:
Saccharomyces cerevisiae acetohydroxyacid synthase
Method: X-RAY DIFFRACTION / Resolution: 3.194 Å

PDB-6wo1:
Hybrid acetohydroxyacid synthase complex structure with Cryptococcus neoformans AHAS catalytic subunit and Saccharomyces cerevisiae AHAS regulatory subunit
Method: X-RAY DIFFRACTION / Resolution: 3.3 Å

Chemicals

ChemComp-TPP:
THIAMINE DIPHOSPHATE / Thiamine pyrophosphate

ChemComp-MG:
Unknown entry

ChemComp-FAD:
FLAVIN-ADENINE DINUCLEOTIDE / FAD*YM / Flavin adenine dinucleotide

ChemComp-60G:
methyl 2-[(4,6-dimethoxypyrimidin-2-yl)carbamoylsulfamoylmethyl]benzoate

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM / Adenosine triphosphate

ChemComp-HOH:
WATER / Water

ChemComp-VAL:
VALINE / Valine

ChemComp-8GF:
2-methylpyrimidin-4-amine

ChemComp-DPO:
DIPHOSPHATE / Pyrophosphate

Source
  • arabidopsis thaliana (thale cress)
  • saccharomyces cerevisiae (brewer's yeast)
  • cryptococcus neoformans (fungus)
KeywordsTRANSFERASE / AHAS / pyruvate / FAD / dioxygen / PLANT PROTEIN / Complex

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