XRD1 Highlights
- XRD1 Highlights
- C1–C4 alcohol–cavitand complexes
- Cuprate Superconductor
- Jack Bean Urease
- XRD1 Sample Changer
- Carbonic Anhydrase
- PDI8CN2
- Human Legumain
- Structure of Human NAPE-PLD
- beta-Chitin in Squid Pen
- Enhanced Green Fluorescent Protein
- Multitarget drug design strategy
- Hydrogen-bonded Organic Pigments
- Selectivity of CNG channels
- Polycyclic Aromatic Hydrocarbons
- Cisplatin Encapsulation within the Ferritin Nanocage
- Crystal structure of the earthworm toxin
- Chemistry at the protein–mineral interface in L-ferritin
- Porous N-doped graphene
- Sliding of the human DNA clamp PCNA
- S1′ Pocket of Thermolysin
- microbial NLP cytolysins
- Human ubiquitin
- Photosynthesis
- Nanoparticles
- Anode Materials
- Stone Materials
- Sensor humidity
- Xe shell
- OSC
- Peptide nanotubes
- Amyloid aggregates
- Perovskites optimization
- Hydrocarbons
- CO2 separation
- Flexibility
- All Pages
Page 4 of 36
Jack Bean Urease
 Folding of the 10-kDa entomotoxic peptide region of JBU (Left) and the corresponding region in B. pasteurii bacterial urease (Right). The insecticidal region in bacterial urease is not intact and consists of two chains.
|
The three dimensional structure of the historic enzyme, the Jack bean urease (JBU) has recently been unraveled. JBU was not only the first enzyme isolated as a crystalline protein by Sumner in 1926, which fetched him the Nobel Prize, but also the first example of a nickel metalloenzyme and the first protein which showed the presence of sulfhydryl groups. Surprisingly, JBU had to wait more than 80 years for its structural revelation |
Retrieve Article
Crystal structure of the first plant urease from jack bean: 83 years of journey from its first crystal to molecular structure; A. Balasubramanian and K. Ponnuraj, J.; Mol. Biol. 400, 274 (2010); 10.1016/j.jmb.2010.05.009 |
Last Updated on Monday, 22 May 2023 15:31
