PDBsum entry 3e2p

Transferase

PDB id: 3e2p

Contents

Protein chains

(+ 6 more) 306 a.a. *

Ligands

SO4 ×4

Waters ×500

* Residue conservation analysis

PDB id:

3e2p

Name:

Transferase

Title:

Catalytic subunit of m. Jannaschii aspartate transcarbamoylase in an orthorhombic crystal form

Structure:

Aspartate carbamoyltransferase. Chain: a, b, c, d, e, f, i, j, k, l, m, n. Fragment: catalytic subunit. Synonym: aspartate transcarbamylase, atcase. Engineered: yes

Source:

Methanocaldococcus jannaschii. Methanococcus jannaschii. Organism_taxid: 2190. Gene: pyrb, mj1581. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

3.00Å R-factor: 0.215 R-free: 0.269

Authors:

J.Vitali,M.J.Colaneri

Key ref:

J.Vitali and M.J.Colaneri (2008). Structure of the catalytic trimer of Methanococcus jannaschii aspartate transcarbamoylase in an orthorhombic crystal form. Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 776-780. PubMed id: 18765902

Date:

06-Aug-08 Release date: 10-Mar-09

Protein chains

Q58976  (PYRB_METJA) -  Aspartate carbamoyltransferase from Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)

Seq: 306 a.a.

Struc: 306 a.a.

Enzyme reactions

• Enzyme class: E.C.2.1.3.2 - aspartate carbamoyltransferase.
• Pathway: Pyrimidine Biosynthesis
• Reaction: carbamoyl phosphate + L-aspartate = N-carbamoyl-L-aspartate + phosphate + H⁺

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

Acta Crystallogr Sect F Struct Biol Cryst Commun 64:776-780 (2008)

PubMed id: 18765902

Structure of the catalytic trimer of Methanococcus jannaschii aspartate transcarbamoylase in an orthorhombic crystal form.

J.Vitali, M.J.Colaneri.

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.