1f2d
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1f2d" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f2d, resolution 2.0Å" /> '''1-AMINOCYCLOPROPANE-1...)
Next diff →
Revision as of 12:25, 20 November 2007
|
1-AMINOCYCLOPROPANE-1-CARBOXYLATE DEAMINASE
Overview
The pyridoxal 5'-phosphate (PLP)-dependent enzyme, 1-aminocyclopropane-1-carboxylate deaminase (ACCD) catalyzes a reaction, that involves a ring opening of cyclopropanoid amino acid, yielding, alpha-ketobutyrate and ammonia. Unlike other PLP-dependent enzymes, this, enzyme has no alpha-hydrogen atom in the substrate. Thus, a unique, mechanism for the bond cleavage is expected. The crystal structure of ACCD, from Hansenula saturnus has been determined at 2.0 A resolution by the, multiple wavelength anomalous diffraction method using mercury atoms as, anomalous scatterers. The model was built on the electron density map, which was obtained by the density averaging of multiple crystal forms. The, final model was refined to an R-factor of 22.5% and an R(free)-factor of, 26.8%. The ACCD folds into two domains, each of which has an open twisted, alpha/beta structure similar to the beta-subunit of tryptophan synthase., However, in ACCD, unlike in other members of the beta family of, PLP-dependent enzymes, PLP is buried deep in the molecule. The structure, provides the first view of the catalytic center of the cyclopropane ring, opening.
About this Structure
1F2D is a Single protein structure of sequence from Williopsis saturnus with SO4 and PLP as ligands. Active as 1-aminocyclopropane-1-carboxylate deaminase, with EC number 3.5.99.7 Full crystallographic information is available from OCA.
Reference
Crystal structure of 1-aminocyclopropane-1-carboxylate deaminase from Hansenula saturnus., Yao M, Ose T, Sugimoto H, Horiuchi A, Nakagawa A, Wakatsuki S, Yokoi D, Murakami T, Honma M, Tanaka I, J Biol Chem. 2000 Nov 3;275(44):34557-65. PMID:10938279
Page seeded by OCA on Tue Nov 20 14:32:43 2007
