Proline utilization A
From Proteopedia
| ||||||||||||
3D Structures of proline utilization A
Updated on 23-October-2017
FunctionProline utilization A (PutA) is a bifunctional flavoprotein which acts as a transcriptional repressor of the put regulon or as a membrane-bound enzyme which catalyzes the oxidation of proline to glutamate. PutA domains include the DNA-binding domain (PRODH), the FAD-dependent proline dehydrogenase domain and the D-pyrroline-5-carboxylate dehydrogenase domain. The binding of proline to the PRODH active site and subsequent reduction of FAD causes a conformation change in PutA and enhance its membrane affinity. As a membrane-bound protein PutA switches from its repressor activity to its enzymatic role[1]. Structural highlightsThe active site residue Tyr540 helps in substrate preference for proline over hydroxyproline. Water molecules shown as red spheres. The 3e2q structure displayed here contains the Tyr540Ser mutant[2].
| ||||||||||||
Updated on 23-October-2017
This page was last modified 13:18, 23 October 2017.