scholarly journals Arginine 54 in the active site of escherichia coli aspartate transcarbamoylase is critical for catalysis: A site-specific mutagenesis, NMR, and X-ray crystallographic study

1992 ◽  
Vol 1 (11) ◽  
pp. 1435-1446 ◽  
Author(s):  
Jeffrey W. Stebbins ◽  
Diane E. Robertson ◽  
Mary F. Roberts ◽  
Raymond C. Stevens ◽  
William N. Lipscomb ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Active Site ◽  
Aspartate Transcarbamoylase ◽  
Site Specific ◽  
X Ray ◽  
Crystallographic Study ◽  
A Site

X-Ray Crystallographic Study of Pyridoxamine 5'-Phosphate-Type Aspartate Aminotransferases from Escherichia coli in Three Forms1

1994 ◽  
Vol 116 (5) ◽  
pp. 1001-1012 ◽  
Author(s):  
Ikuko Miyahara ◽  
Ken Hirotsu ◽  
Hideyuki Hayashi ◽  
Hiroyuki Kagamiyama
Keyword(s):  
Escherichia Coli ◽  
X Ray ◽  
Crystallographic Study

X-Ray Crystallographic Study of Pyridoxal 5′-Phosphate-Type Aspartate Aminotransferases from Escherichia coli in Open and Closed Form1

1994 ◽  
Vol 116 (1) ◽  
pp. 95-107 ◽  
Author(s):  
Akihiro Okamoto ◽  
Taiichi Higuchi ◽  
Ken Hirotsu ◽  
Seiki Kuramitsu ◽  
Hiroyuki Kagamiyama
Keyword(s):  
Escherichia Coli ◽  
X Ray ◽  
Crystallographic Study

scholarly journals Ligand interactions at the active site of aspartate transcarbamoylase from Escherichia coli

Biochemistry ◽  
1986 ◽  
Vol 25 (7) ◽  
pp. 1605-1611 ◽  
Author(s):  
Paul R. Dennis ◽  
M. Vijaya Krishna ◽  
Maria Di Gregorio ◽  
William W. C. Chan
Keyword(s):  
Escherichia Coli ◽  
Active Site ◽  
Aspartate Transcarbamoylase ◽  
Ligand Interactions

scholarly journals (−)-Homosalinosporamide A and Its Mode of Proteasome Inhibition: An X-ray Crystallographic Study

Marine Drugs ◽  
2018 ◽  
Vol 16 (7) ◽  
pp. 240 ◽  
Author(s):  
Michael Groll ◽  
Henry Nguyen ◽  
Sreekumar Vellalath ◽  
Daniel Romo
Keyword(s):  
Natural Product ◽  
Active Site ◽  
Late Stage ◽  
Enzyme Assay ◽  
Proteasome Inhibition ◽  
Fine Tuning ◽  
Synthetic Approach ◽  
X Ray ◽  
Salinosporamide A ◽  
Crystallographic Study

Upon acylation of the proteasome by the β-lactone inhibitor salinosporamide A (SalA), tetrahydrofuran formation occurs by intramolecular alkylation of the incipient alkoxide onto the choroethyl sidechain and irreversibly blocks the active site. Our previously described synthetic approach to SalA, utilizing a bioinspired, late-stage, aldol-β-lactonization strategy to construct the bicyclic β-lactone core, enabled synthesis of (–)-homosalinosporamide A (homoSalA). This homolog was targeted to determine whether an intramolecular tetrahydropyran is formed in a similar manner to SalA. Herein, we report the X-ray structure of the yeast 20S proteasome:homoSalA-complex which reveals that tetrahydropyran ring formation does not occur despite comparable potency at the chymotrypsin-like active site in a luminogenic enzyme assay. Thus, the natural product derivative homoSalA blocks the proteasome by a covalent reversible mode of action, opening the door for further fine-tuning of proteasome inhibition.

scholarly journals Engineering a light-controlled F1ATPase using structure-based protein design

PeerJ ◽  
2016 ◽  
Vol 4 ◽  
pp. e2286 ◽  
Author(s):  
Daniel Hoersch
Keyword(s):  
Protein Design ◽  
Active Site ◽  
Atp Hydrolysis ◽  
Site Specific ◽  
Dynamic Constraint ◽  
End Distance ◽  
A Site ◽  
Hydrolysis Activity

The F1sub-complex of ATP synthase is a biological nanomotor that converts the free energy of ATP hydrolysis into mechanical work with an astonishing efficiency of up to 100% (Kinosita et al., 2000). To probe the principal mechanics of the machine, I re-engineered the active site ofE.coliF1ATPase with a structure-based protein design approach: by incorporation of a site-specific, photoswitchable crosslinker, whose end-to-end distance can be modulated by illumination with light of two different wavelengths, a dynamic constraint was imposed on the inter-atomic distances of the α and β subunits. Crosslinking reduced the ATP hydrolysis activity of four designs tested in vitro and in one case created a synthetic ATPase whose activity can be reversibly modulated by subsequent illumination with near UV and blue light. The work is a first step into the direction of the long-term goal to design nanoscaled machines based on biological parts that can be precisely controlled by light.

Sign in / Sign up

Export Citation Format

Share Document