2QDY

Crystal Structure of Fe-type NHase from Rhodococcus erythropolis AJ270

Summary for 2QDY

• Entry DOI: 10.2210/pdb2qdy/pdb
• Related: 2AHJ
• Descriptor: Nitrile hydratase subunit alpha, Nitrile hydratase subunit beta, FE (III) ION, ... (8 entities in total)
• Functional Keywords: nitrile hydratase, post translation, lyase
• Biological source: Rhodococcus erythropolis; More
• Total number of polymer chains: 2
• Total formula weight: 47491.64

Authors

Song, L.,Shi, J.,Xue, Z.,Wang, M.-X.,Qian, S. (deposition date: 2007-06-22, release date: 2008-05-13, Last modification date: 2024-10-30)

Primary citation

Song, L.,Wang, M.,Shi, J.,Xue, Z.,Wang, M.-X.,Qian, S.
High resolution X-ray molecular structure of the nitrile hydratase from Rhodococcus erythropolis AJ270 reveals posttranslational oxidation of two cysteines into sulfinic acids and a novel biocatalytic nitrile hydration mechanism
Biochem.Biophys.Res.Commun., 362:319-324, 2007

PubMed Abstract: The crystal structure of Fe-type nitrile hydratase from Rhodococcus erythropolis AJ270 was determined at 1.3A resolution. The two cysteine residues (alphaCys(112) and alphaCys(114)) equatorially coordinated to the ferric ion were post-translationally modified to cysteine sulfinic acids. A glutamine residue (alphaGln(90)) in the active center gave double conformations. Based on the interactions among the enzyme, substrate and water molecules, a new mechanism of biocatalysis of nitrile hydratase was proposed, in which the water molecule activated by the glutamine residue performed as the nucleophile to attack on the nitrile which was simultaneously interacted by another water molecule coordinated to the ferric ion.

PubMed: 17716629
DOI: 10.1016/j.bbrc.2007.07.184

Experimental method

X-RAY DIFFRACTION (1.3 Å)