Metal-free form of Pseudomonas stutzeri L-rhamnose isomerase

Catalytic reaction mechanism of Pseudomonas stutzeri l-rhamnose isomerase deduced from X-ray structures

The structures of L-rhamnose isomerase from Pseudomonas stutzeri in complexes with L-rhamnose and D-allose provide insights into broad substrate specificity

7-8% (W/V) polyethylene glycol 20000, 50mM MES, pH 6.3, VAPOR DIFFUSION, HANGING DROP, temperature 298K

The enzyme (D150N)complexed with L-rhamnose

The enzyme (D150N)complexed with D-allose

The enzyme (D150N, D327N) with L-rhamnulose (ring conformation)

The enzyme (D150N, D327N) with D-psicose (ring conformation)

The enzyme (D150N, S329K) with L-rhamnose (open conformation)

The enzyme (D150N, S329K) with D-psicose (open conformation)

BETA/ALPHA BARREL, HOMO-TETRAMER, METAL-BINDING PROTEIN, TIM barrel, Isomerase