1GVG
Crystal Structure of Clavaminate Synthase with Nitric Oxide
Summary for 1GVG
| Entry DOI | 10.2210/pdb1gvg/pdb |
| Related | 1DRT 1DRY 1DS0 1DS1 |
| Descriptor | CLAVAMINATE SYNTHASE 1, FE (III) ION, 2-OXOGLUTARIC ACID, ... (7 entities in total) |
| Functional Keywords | oxidoreductase, lyase, oxygenase, trifunctional enzyme, clavaminate synthase 1, jelly roll, nitric oxide |
| Biological source | STREPTOMYCES CLAVULIGERUS |
| Total number of polymer chains | 1 |
| Total formula weight | 36167.19 |
| Authors | Zhang, Z.H.,Ren, J.,McKinnon, C.H.,Clifton, I.J.,Harlos, K.,Schofield, C.J. (deposition date: 2002-02-12, release date: 2003-02-07, Last modification date: 2023-12-13) |
| Primary citation | Zhang, Z.H.,Ren, J.,Harlos, K.,McKinnon, C.H.,Clifton, I.J.,Schofield, C.J. Crystal Structure of a Clavaminate Synthase-Fe(II) -2-Oxoglutarate-Substrate-No Complex: Evidence for Metal Centered Rearrangements FEBS Lett., 517:7-, 2002 Cited by PubMed Abstract: Clavaminate synthase (CAS), a 2-oxoglutarate (2OG) dependent dioxygenase, catalyses three steps in the biosynthesis of clavulanic acid. Crystals of CAS complexed with Fe(II), 2OG and deoxyguanidinoproclavaminate were exposed to nitric oxide (NO) acting as a dioxygen analogue. Prior to exposure with NO, the active site Fe(II) is octahedrally coordinated by a water molecule, the 2-oxo and 1-carboxylate groups of 2OG, and the side-chains of an aspartyl and two histidinyl residues. NO binds to the position previously occupied by the 2OG 1-carboxylate concomitant with rearrangement of the latter to the position previously occupied by the displaced water. PubMed: 12062399DOI: 10.1016/S0014-5793(02)02520-6 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.54 Å) |
Structure validation
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