Open AccessStructure of the catalytic trimer of Methanococcus jannaschii aspartate transcarbamoylase in an orthorhombic crystal form
Author(s) -
Vitali Jacqueline,
Colaneri Michael J.
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108025359
Subject(s) - methanococcus , orthorhombic crystal system , trimer , monoclinic crystal system , crystallography , aspartate carbamoyltransferase , crystal structure , crystal (programming language) , chemistry , stereochemistry , materials science , dimer , organic chemistry , archaea , allosteric regulation , biochemistry , enzyme , computer science , programming language , gene
Crystals of the catalytic subunit of Methanococcus jannaschii aspartate transcarbamoylase in an orthorhombic crystal form contain four crystallographically independent trimers which associate in pairs to form stable staggered complexes that are similar to each other and to a previously determined monoclinic C 2 form. Each subunit has a sulfate in the central channel. The catalytic subunits in these complexes show flexibility, with the elbow angles of the monomers differing by up to 7.4° between crystal forms. Moreover, there is also flexibility in the relative orientation of the trimers around their threefold axis in the complexes, with a difference of 4° between crystal forms.