1dw9
From Proteopedia
STRUCTURE OF CYANASE REVEALS THAT A NOVEL DIMERIC AND DECAMERIC ARRANGEMENT OF SUBUNITS IS REQUIRED FOR FORMATION OF THE ENZYME ACTIVE SITE
Template:ABSTRACT PUBMED 10801492
About this Structure
1dw9 is a 10 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
- Walsh MA, Otwinowski Z, Perrakis A, Anderson PM, 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. 2000 May 15;8(5):505-14. PMID:10801492
- Sung YC, Anderson PM, Fuchs JA. Characterization of high-level expression and sequencing of the Escherichia coli K-12 cynS gene encoding cyanase. J Bacteriol. 1987 Nov;169(11):5224-30. PMID:2822670
- Anderson PM, Little RM. Kinetic properties of cyanase. Biochemistry. 1986 Apr 8;25(7):1621-6. PMID:3518792
- Anderson PM, Johnson WV, Endrizzi JA, Little RM, Korte JJ. Interaction of mono- and dianions with cyanase: evidence for apparent half-site binding. Biochemistry. 1987 Jun 30;26(13):3938-43. PMID:3651424
- Anderson PM. Purification and properties of the inducible enzyme cyanase. Biochemistry. 1980 Jun 24;19(13):2882-8. PMID:6994799
Categories: Cyanase | Escherichia coli | Anderson, P M. | Joachimiak, A. | Mcsg, Midwest Center for Structural Genomics. | Otwinowski, Z. | Perrakis, A. | Walsh, M A. | Cyanate degradation | Lyase | Mcsg | Midwest center for structural genomic | Protein structure initiative | Psi | Structural genomic
