1V29

Crystal structure of Nitrile hydratase from a thermophile Bacillus smithii

Summary for 1V29

• Entry DOI: 10.2210/pdb1v29/pdb
• Related: 1AHJ 1IRE 2AHJ
• Descriptor: nitrile hydratase a chain, nitrile hydratase b chain, COBALT (II) ION, ... (4 entities in total)
• Functional Keywords: nhase, bacillus smithii, lyase
• Biological source: Bacillus smithii; More
• Total number of polymer chains: 2
• Total formula weight: 52175.24

Authors

Hourai, S.,Miki, M.,Takashima, Y.,Mitsuda, S.,Yanagi, K. (deposition date: 2003-10-09, release date: 2004-10-09, Last modification date: 2023-12-27)

Primary citation

Hourai, S.,Miki, M.,Takashima, Y.,Mitsuda, S.,Yanagi, K.
Crystal structure of nitrile hydratase from a thermophilic Bacillus smithii
Biochem.Biophys.Res.Commun., 312:340-345, 2003

PubMed Abstract: The crystal structure of the nitrile hydratase (NHase) from Bacillus smithii SC-J05-1 was determined. Our analysis of the structure shows that some residues that seem to be responsible for substrate recognition are different from those of other NHases. In particular, the Phe52 in the beta subunit of NHase from B. smithii covers the metal center partially like a small lid and narrows the active site cleft. It is well known that the NHase from B. smithii especially prefers aliphatic nitriles for its substrate rather than aromatic ones, and we can now infer that the Phe52 residue may play a key role in the substrate specificity for this enzyme. This finding leads us to suggest that substitution of these residues may alter the substrate specificity of the enzyme.

PubMed: 14637142
DOI: 10.1016/j.bbrc.2003.10.124

Experimental method

X-RAY DIFFRACTION (2.6 Å)