scholarly journals Crystal structure of gene locus At3g16990 from Arabidopsis thaliana

2004 ◽  
Vol 57 (1) ◽  
pp. 221-222 ◽  
Author(s):  
Paul G. Blommel ◽  
David W. Smith ◽  
Craig A. Bingman ◽  
David H. Dyer ◽  
Ivan Rayment ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Arabidopsis Thaliana ◽  
Gene Locus

Crystal structure of tubulin folding cofactor A from Arabidopsis thaliana and its β-tubulin binding characterization

FEBS Letters ◽  
2010 ◽  
Vol 584 (16) ◽  
pp. 3533-3539 ◽  
Author(s):  
Lu Lu ◽  
Jie Nan ◽  
Wei Mi ◽  
Lan-Fen Li ◽  
Chun-Hong Wei ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Arabidopsis Thaliana ◽  
Tubulin Binding ◽  
Β Tubulin

scholarly journals Structural and functional studies of Arabidopsis thaliana legumain beta reveal isoform specific mechanisms of activation and substrate recognition

2020 ◽  
Vol 295 (37) ◽  
pp. 13047-13064 ◽  
Author(s):  
Elfriede Dall ◽  
Florian B. Zauner ◽  
Wai Tuck Soh ◽  
Fatih Demir ◽  
Sven O. Dahms ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Arabidopsis Thaliana ◽  
Cyclic Peptides ◽  
Molecular Mechanisms ◽  
Functional Studies ◽  
Plant Characteristic ◽  
Activation Mechanisms ◽  
Binding Pockets ◽  
First Time ◽  
Autocatalytic Activation

The vacuolar cysteine protease legumain plays important functions in seed maturation and plant programmed cell death. Because of their dual protease and ligase activity, plant legumains have become of particular biotechnological interest, e.g. for the synthesis of cyclic peptides for drug design or for protein engineering. However, the molecular mechanisms behind their dual protease and ligase activities are still poorly understood, limiting their applications. Here, we present the crystal structure of Arabidopsis thaliana legumain isoform β (AtLEGβ) in its zymogen state. Combining structural and biochemical experiments, we show for the first time that plant legumains encode distinct, isoform-specific activation mechanisms. Whereas the autocatalytic activation of isoform γ (AtLEGγ) is controlled by the latency-conferring dimer state, the activation of the monomeric AtLEGβ is concentration independent. Additionally, in AtLEGβ the plant-characteristic two-chain intermediate state is stabilized by hydrophobic rather than ionic interactions, as in AtLEGγ, resulting in significantly different pH stability profiles. The crystal structure of AtLEGβ revealed unrestricted nonprime substrate binding pockets, consistent with the broad substrate specificity, as determined by degradomic assays. Further to its protease activity, we show that AtLEGβ exhibits a true peptide ligase activity. Whereas cleavage-dependent transpeptidase activity has been reported for other plant legumains, AtLEGβ is the first example of a plant legumain capable of linking free termini. The discovery of these isoform-specific differences will allow us to identify and rationally design efficient ligases with application in biotechnology and drug development.

Crystal structure of Arabidopsis thaliana RabA1a

2018 ◽  
Vol 61 (2) ◽  
pp. 93-109 ◽  
Author(s):  
Ji-Sook Yun ◽  
Sung Chul Ha ◽  
Shinae Kim ◽  
Yeon-Gil Kim ◽  
Hyeran Kim ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Arabidopsis Thaliana

scholarly journals Crystal structure of the protein A t3g01520, a eukaryotic universal stress protein‐like protein from arabidopsis thaliana in complex with AMP

2015 ◽  
Vol 83 (7) ◽  
pp. 1368-1373 ◽  
Author(s):  
Do Jin Kim ◽  
Eduard Bitto ◽  
Craig A. Bingman ◽  
Hyun‐Jung Kim ◽  
Byung Woo Han ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Arabidopsis Thaliana ◽  
Protein A ◽  
Stress Protein ◽  
Universal Stress Protein

scholarly journals Crystal structure of Arabidopsis thaliana HPPK/DHPS, a bifunctional enzyme and target of the herbicide asulam

2021 ◽  
Author(s):  
Grishma Vadlamani ◽  
Kirill V Sukhoverkov ◽  
Joel Haywood ◽  
Karen J Breese ◽  
Mark F Fisher ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Arabidopsis Thaliana ◽  
Mode Of Action ◽  
Rational Design ◽  
Binding Pocket ◽  
Structural Basis ◽  
Metabolic Resistance ◽  
Folate Biosynthesis ◽  
Limited Opportunity ◽  
Regulatory Scrutiny

Herbicides are vital for modern agriculture, but their utility is threatened by genetic or metabolic resistance in weeds as well as heightened regulatory scrutiny. Of the known herbicide modes of action, 6-hydroxymethyl-7,8-dihydropterin synthase (DHPS) which is involved in folate biosynthesis, is targeted by just one commercial herbicide, asulam. A mimic of the substrate para-aminobenzoic acid, asulam is chemically similar to sulfonamide antibiotics - and while still in widespread use, asulam has faced regulatory scrutiny. With an entire mode of action represented by just one commercial agrochemical, we sought to improve the understanding of its plant target. Here we solve a 2.6 Å resolution crystal structure for Arabidopsis thaliana DHPS that is conjoined to 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase (HPPK) and reveal a strong structural conservation with bacterial counterparts at the sulfonamide-binding pocket of DHPS. We demonstrate asulam and the antibiotics sulfacetamide and sulfamethoxazole have herbicidal as well as antibacterial activity and explore the structural basis of their potency by modelling these compounds in mitochondrial HPPK/DHPS. Our findings suggest limited opportunity for the rational design of plant selectivity from asulam and that pharmacokinetic or delivery differences between plants and microbes might be the best approaches to safeguard this mode of action.

Crystal structure of the TL29 protein from Arabidopsis thaliana: An APX homolog without peroxidase activity

2011 ◽  
Vol 176 (1) ◽  
pp. 24-31 ◽  
Author(s):  
Erik Lundberg ◽  
Patrik Storm ◽  
Wolfgang P. Schröder ◽  
Christiane Funk
Keyword(s):  
Crystal Structure ◽  
Arabidopsis Thaliana ◽  
Peroxidase Activity

scholarly journals Crystal structure of Psb27 from Arabidopsis thaliana determined at a resolution of 1.85 Å

2017 ◽  
Vol 136 (2) ◽  
pp. 139-146 ◽  
Author(s):  
Cheng Xingxing ◽  
Liu Jiuyang ◽  
Zhang Huan ◽  
Li Fudong ◽  
Zhang Shuya ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Arabidopsis Thaliana
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