1afw
From Proteopedia
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THE 1.8 ANGSTROM CRYSTAL STRUCTURE OF THE DIMERIC PEROXISOMAL THIOLASE OF SACCHAROMYCES CEREVISIAE
Overview
The dimeric, peroxisomal 3-ketoacyl-CoA thiolase catalyses the conversion, of 3-ketoacyl-CoA into acyl-CoA, which is shorter by two carbon atoms., This reaction is the last step of the beta-oxidation pathway. The crystal, structure of unliganded peroxisomal thiolase of the yeast Saccharomyces, cerevisiae has been refined at 1.8 A resolution. An unusual feature of, this structure is the presence of two helices, completely buried in the, dimer and sandwiched between two beta-sheets. The analysis of the, structure shows that the sequences of these helices are not hydrophobic, but generate two amphipathic helices. The helix in the N-terminal domain, exposes the polar side-chains to a cavity at the dimer interface, filled, with structured water molecules. The central helix in the C-terminal, ... [(full description)]
About this Structure
1AFW is a [Single protein] structure of sequence from [Saccharomyces cerevisiae] with MRD as [ligand]. Active as [Acetyl-CoA C-acyltransferase], with EC number [2.3.1.16]. Structure known Active Sites: AVA and AVB. Full crystallographic information is available from [OCA].
Reference
The 1.8 A crystal structure of the dimeric peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae: implications for substrate binding and reaction mechanism., Mathieu M, Modis Y, Zeelen JP, Engel CK, Abagyan RA, Ahlberg A, Rasmussen B, Lamzin VS, Kunau WH, Wierenga RK, J Mol Biol. 1997 Oct 31;273(3):714-28. PMID:9402066
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