5zyr
From Proteopedia
Crystal structure of the reductase (C1) component of p-hydroxyphenylacetate 3-hydroxylase (HPAH) from Acinetobacter baumannii
Structural highlights
Function[HPAHR_ACIBA] Reductase component of a two-component system that supplies reduced FMN (FMNH2) to the oxygenase component to catalyze the hydroxylation of 4-hydroxyphenylacetic acid, leading to the production of 3,4-dihydroxyphenylacetate (3,4-DHPA). Catalyzes the reduction of free flavins (FMN, FAD and riboflavin) by NADH. Subsequently, the reduced flavins diffuse to the oxygenase component C2.[1] [2] [3] Publication Abstract from PubMedp-Hydroxyphenylacetate 3-hydroxylase (HPAH) from Acinetobacter baumannii catalyzes the hydroxylation of p-hydroxyphenylacetate (HPA) at the ortho position to yield 3,4-dihydroxyphenylacetate (DHPA). HPAH from A. baumannii is a two-component flavoprotein consisting of a smaller reductase (C(1)) component and a larger oxygenase (C(2)) component. The C(1) component supplies a reduced flavin in its free form to the C(2) counterpart for hydroxylation. In addition, HPA can bind to C(1) and enhance the flavin-reduction rate without becoming hydroxylated. The recombinant C(1) component was purified and crystallized using the microbatch method at 295 K. X-ray diffraction data were collected to 2.3 A resolution using synchrotron radiation on the BL13B1 beamline at NSRRC, Taiwan. The crystal belonged to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 47.78, b = 59.92, c = 211.85 A, and contained two molecules of C(1) per asymmetric unit. Crystallization and preliminary X-ray analysis of the reductase component of p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii.,Oonanant W, Sucharitakul J, Chaiyen P, Yuvaniyama J Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Jun 1;68(Pt 6):720-3. doi:, 10.1107/S1744309112016909. Epub 2012 May 24. PMID:22684080[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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