6ALQ
VioC L-arginine hydroxylase bound to Fe(II), L-arginine, and succinate
Summary for 6ALQ
| Entry DOI | 10.2210/pdb6alq/pdb |
| Descriptor | Alpha-ketoglutarate-dependent L-arginine hydroxylase, FE (II) ION, SUCCINIC ACID, ... (5 entities in total) |
| Functional Keywords | hydroxylase, 2-oxo-glutarate, iron, oxidoreductase |
| Biological source | Streptomyces vinaceus |
| Total number of polymer chains | 1 |
| Total formula weight | 43659.56 |
| Authors | Dunham, N.P.,Mitchell, A.J.,Boal, A.K. (deposition date: 2017-08-08, release date: 2017-09-06, Last modification date: 2024-03-13) |
| Primary citation | Mitchell, A.J.,Dunham, N.P.,Martinie, R.J.,Bergman, J.A.,Pollock, C.J.,Hu, K.,Allen, B.D.,Chang, W.C.,Silakov, A.,Bollinger, J.M.,Krebs, C.,Boal, A.K. Visualizing the Reaction Cycle in an Iron(II)- and 2-(Oxo)-glutarate-Dependent Hydroxylase. J. Am. Chem. Soc., 139:13830-13836, 2017 Cited by PubMed Abstract: Iron(II)- and 2-(oxo)-glutarate-dependent oxygenases catalyze diverse oxidative transformations that are often initiated by abstraction of hydrogen from carbon by iron(IV)-oxo (ferryl) complexes. Control of the relative orientation of the substrate C-H and ferryl Fe-O bonds, primarily by direction of the oxo group into one of two cis-related coordination sites (termed inline and offline), may be generally important for control of the reaction outcome. Neither the ferryl complexes nor their fleeting precursors have been crystallographically characterized, hindering direct experimental validation of the offline hypothesis and elucidation of the means by which the protein might dictate an alternative oxo position. Comparison of high-resolution X-ray crystal structures of the substrate complex, an Fe(II)-peroxysuccinate ferryl precursor, and a vanadium(IV)-oxo mimic of the ferryl intermediate in the l-arginine 3-hydroxylase, VioC, reveals coordinated motions of active site residues that appear to control the intermediate geometries to determine reaction outcome. PubMed: 28823155DOI: 10.1021/jacs.7b07374 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.67 Å) |
Structure validation
Download full validation report
