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

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: 12062399
DOI: 10.1016/S0014-5793(02)02520-6

Experimental method

X-RAY DIFFRACTION (1.54 Å)