Eong Cheah

TL;DR: The alpha/beta hydrolase fold as mentioned in this paper is common to several hydrolytic enzymes of widely differing phylogenetic origin and catalytic function, including the serine protease catalytic triad.

TL;DR: The X-ray structure of GlnK is crystallised and solved at 2.0 A resolution and suggests that the T-loops do not have a rigid structure and that they may be flexible in solution.

TL;DR: The structure of PII suggests potential regions of interaction with other proteins and serves as an initial step in understanding its signal transducing role in nitrogen regulation.

TL;DR: The structure of the bacterial signal transduction protein P(II) has been refined to an R factor of 13.2% using 3sigma data between 10 and 1.9 A, confirming the correctness of the 2.7 A model, although it leads to a redefinition of the extent of various secondary-structural elements.

TL;DR: The 3D structure of PII, the central protein that controls the level of transcription and the enzymatic activity of glutamine synthetase in enteric bacteria, revealed that residues 37–55 form the ‘T’ loop, part of which protrudes from the core of the protein, and suggests a role for this residue in recognition and binding of the sensor enzyme uridylyl transferase.