3GJB

CytC3 with Fe(II) and alpha-ketoglutarate

Summary for 3GJB

• Entry DOI: 10.2210/pdb3gjb/pdb
• Related: 3GJA
• Descriptor: CytC3, FE (II) ION, 2-OXOGLUTARIC ACID, ... (6 entities in total)
• Functional Keywords: cytc3, halogenase, beta barrel, biosynthetic protein
• Biological source: Streptomyces sp.
• Total number of polymer chains: 2
• Total formula weight: 74183.61

Authors

Wong, C.,Drennan, C.L. (deposition date: 2009-03-08, release date: 2009-04-14, Last modification date: 2024-02-21)

Primary citation

Wong, C.,Fujimori, D.G.,Walsh, C.T.,Drennan, C.L.
Structural analysis of an open active site conformation of nonheme iron halogenase CytC3
J.Am.Chem.Soc., 131:4872-4879, 2009

PubMed Abstract: CytC3, a member of the recently discovered class of nonheme Fe(II) and alpha-ketoglutarate (alphaKG)-dependent halogenases, catalyzes the double chlorination of L-2-aminobutyric acid (Aba) to produce a known Streptomyces antibiotic, gamma,gamma-dichloroaminobutyrate. Unlike the majority of the Fe(II)-alphaKG-dependent enzymes that catalyze hydroxylation reactions, halogenases catalyze a transfer of halides. To examine the important enzymatic features that discriminate between chlorination and hydroxylation, the crystal structures of CytC3 both with and without alphaKG/Fe(II) have been solved to 2.2 A resolution. These structures capture CytC3 in an open active site conformation, in which no chloride is bound to iron. Comparison of the open conformation of CytC3 with the closed conformation of another nonheme iron halogenase, SyrB2, suggests two important criteria for creating an enzyme-bound Fe-Cl catalyst: (1) the presence of a hydrogen-bonding network between the chloride and surrounding residues, and (2) the presence of a hydrophobic pocket in which the chloride resides.

PubMed: 19281171
DOI: 10.1021/ja8097355

Experimental method

X-RAY DIFFRACTION (2.2 Å)