1DWK

STRUCTURE OF CYANASE WITH THE DI-ANION OXALATE BOUND AT THE ENZYME ACTIVE SITE

Summary for 1DWK

• Entry DOI: 10.2210/pdb1dwk/pdb
• Related: 1DW9
• Descriptor: CYANATE HYDRATASE, SULFATE ION, OXALATE ION, ... (4 entities in total)
• Functional Keywords: lyase, cyanate degradation, psi, protein structure initiative, midwest center for structural genomics, mcsg
• Biological source: ESCHERICHIA COLI
• Total number of polymer chains: 10
• Total formula weight: 175203.31

Authors

Walsh, M.A.,Otwinowski, Z.,Perrakis, A.,Anderson, P.M.,Joachimiak, A. (deposition date: 1999-12-07, release date: 2000-05-16, Last modification date: 2024-10-23)

Primary citation

Walsh, M.A.,Otwinowski, Z.,Perrakis, A.,Anderson, P.M.,Joachimiak, A.
Structure of Cyanase Reveals that a Novel Dimeric and Decameric Arrangement of Subunits is Required for Formation of the Enzyme Active Site.
Structure, 8:505-, 2000

PubMed Abstract: Cyanase is an enzyme found in bacteria and plants that catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide. In Escherichia coli, cyanase is induced from the cyn operon in response to extracellular cyanate. The enzyme is functionally active as a homodecamer of 17 kDa subunits, and displays half-site binding of substrates or substrate analogs. The enzyme shows no significant amino acid sequence homology with other proteins.

PubMed: 10801492
DOI: 10.1016/S0969-2126(00)00134-9

Experimental method

X-RAY DIFFRACTION (1.65 Å)