3E2P
Catalytic subunit of M. Jannaschii aspartate transcarbamoylase in an orthorhombic crystal form
Summary for 3E2P
Entry DOI | 10.2210/pdb3e2p/pdb |
Descriptor | Aspartate carbamoyltransferase, SULFATE ION (3 entities in total) |
Functional Keywords | aspartate transcarbamoylase, atcase, pyrimidine biosynthesis, thermostability, methanococcus jannaschii, transferase |
Biological source | Methanocaldococcus jannaschii (Methanococcus jannaschii) |
Total number of polymer chains | 12 |
Total formula weight | 422911.70 |
Authors | Vitali, J.,Colaneri, M.J. (deposition date: 2008-08-06, release date: 2009-03-10, Last modification date: 2023-08-30) |
Primary citation | Vitali, J.,Colaneri, M.J. Structure of the catalytic trimer of Methanococcus jannaschii aspartate transcarbamoylase in an orthorhombic crystal form. Acta Crystallogr.,Sect.F, 64:776-780, 2008 Cited by PubMed Abstract: 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 C2 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 degrees 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 degrees between crystal forms. PubMed: 18765902DOI: 10.1107/S1744309108025359 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
Download full validation report
