PDBsum entry 4a6r

Transferase

PDB id: 4a6r

Contents

Protein chains

423 a.a.

Ligands

TA8 ×2

Waters ×842

PDB id:

4a6r

Name:

Transferase

Title:

Crystal structure of the omega transaminase from chromobacterium violaceum in the apo form, crystallised from polyacrylic acid

Structure:

Omega transaminase. Chain: a, b. Synonym: probable aminotransferase. Engineered: yes

Source:

Chromobacterium violaceum. Organism_taxid: 536. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

1.35Å R-factor: 0.135 R-free: 0.163

Authors:

D.T.Logan,M.Hakansson,K.Yengo,M.Svedendahl Humble,K.Engelmark Cassimjee,B.Walse,V.Abedi,H.-J.Federsel,P.Berglund

Key ref:

M.S.Humble et al. (2012). Crystal structures of the Chromobacterium violaceumω-transaminase reveal major structural rearrangements upon binding of coenzyme PLP. Febs J, 279, 779-792. PubMed id: 22268978

Date:

08-Nov-11 Release date: 25-Jan-12

Protein chains

Q7NWG4  (Q7NWG4_CHRVO) -  Probable aminotransferase from Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / CCUG 213 / NBRC 12614 / NCIMB 9131 / NCTC 9757 / MK)

Seq: 459 a.a.

Struc: 423 a.a.

Enzyme reactions

• Enzyme class: E.C.2.6.1.62 - adenosylmethionine--8-amino-7-oxononanoate transaminase.
• Reaction: (8S)-8-amino-7-oxononanoate + S-adenosyl-L-methionine = S-adenosyl-4- methylsulfanyl-2-oxobutanoate + (7R,8S)-7,8-diammoniononanoate
• Cofactor: Pyridoxal 5'-phosphate

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

Added reference

Febs J 279:779-792 (2012)

PubMed id: 22268978

Crystal structures of the Chromobacterium violaceumω-transaminase reveal major structural rearrangements upon binding of coenzyme PLP.

M.S.Humble, K.E.Cassimjee, M.Håkansson, Y.R.Kimbung, B.Walse, V.Abedi, H.J.Federsel, P.Berglund, D.T.Logan.

ABSTRACT

The bacterial ω-transaminase from Chromobacterium violaceum (Cv-ωTA, EC2.6.1.18) catalyses industrially important transamination reactions by use of the coenzyme pyridoxal 5'-phosphate (PLP). Here, we present four crystal structures of Cv-ωTA: two in the apo form, one in the holo form and one in an intermediate state, at resolutions between 1.35 and 2.4 Å. The enzyme is a homodimer with a molecular mass of ∼ 100 kDa. Each monomer has an active site at the dimeric interface that involves amino acid residues from both subunits. The apo-Cv-ωTA structure reveals unique 'relaxed' conformations of three critical loops involved in structuring the active site that have not previously been seen in a transaminase. Analysis of the four crystal structures reveals major structural rearrangements involving elements of the large and small domains of both monomers that reorganize the active site in the presence of PLP. The conformational change appears to be triggered by binding of the phosphate group of PLP. Furthermore, one of the apo structures shows a disordered 'roof ' over the PLP-binding site, whereas in the other apo form and the holo form the 'roof' is ordered. Comparison with other known transaminase crystal structures suggests that ordering of the 'roof' structure may be associated with substrate binding in Cv-ωTA and some other transaminases. DATABASE: The atomic coordinates and structure factors for the Chromobacterium violaceumω-transaminase crystal structures can be found in the RCSB Protein Data Bank (http://www.rcsb.org) under the accession codes 4A6U for the holoenzyme, 4A6R for the apo1 form, 4A6T for the apo2 form and 4A72 for the mixed form STRUCTURED DIGITAL ABSTRACT: •  -transaminases and -transaminases bind by dynamic light scattering (View interaction) • -transaminase and -transaminase bind by x-ray crystallography (View interaction) • -transaminase and -transaminase bind by x-ray crystallography (View interaction).