2DXB

Recombinant thiocyanate hydrolase comprising partially-modified cobalt centers

Summary for 2DXB

• Entry DOI: 10.2210/pdb2dxb/pdb
• Related: 2DD4 2DD5 2DXC
• Descriptor: Thiocyanate hydrolase subunit alpha, Thiocyanate hydrolase subunit beta, Thiocyanate hydrolase subunit gamma, ... (6 entities in total)
• Functional Keywords: hydrolase, cobalt, metalloprotein, sulfenic acid, sulfinic acid, nitrile hydratase, thiocyanate, carbonyl sulfide, claw setting, protein, enzyme, complex, model complex, non-corrin, post-translational modification, sulfenate, sulfinate
• Biological source: Thiobacillus thioparus; More
• Total number of polymer chains: 24
• Total formula weight: 482768.28

Authors

Arakawa, T.,Kawano, Y.,Katayama, Y.,Yohda, M.,Odaka, M. (deposition date: 2006-08-25, release date: 2007-08-28, Last modification date: 2024-10-23)

Primary citation

Arakawa, T.,Kawano, Y.,Katayama, Y.,Nakayama, H.,Dohmae, N.,Yohda, M.,Odaka, M.
Structural Basis for Catalytic Activation of Thiocyanate Hydrolase Involving Metal-Ligated Cysteine Modification
J.Am.Chem.Soc., 131:14838-14843, 2009

PubMed Abstract: Thiocyanate hydrolase (SCNase) is a member of a family of nitrile hydratase proteins, each of which contains a unique noncorrin cobalt center with two post-translationally modified cysteine ligands, cysteine-sulfenic acid or -sulfenate (Cys-SO(H)), and cysteine-sulfininate (Cys-SO(2)(-)), respectively. We have found that a partially matured recombinant SCNase was activated during storage. The crystal structures of SCNase before and after storage demonstrated that Cys-SO(2)(-) modification of gammaCys131 proceeded to completion prior to storage, while Cys-SO(H) modification of gammaCys133 occurred during storage. SCNase activity was suppressed when gammaCys133 was further oxidized to Cys-SO(2)(-). The correlation between the catalytic activity and the extent of the gammaCys133 modification indicates that the cysteine sulfenic acid modification of gammaCys133 is of primary importance in determining the activity of SCNase.

PubMed: 19785438
DOI: 10.1021/ja903979s

Experimental method

X-RAY DIFFRACTION (2.25 Å)