PDBsum entry 1w3d

Transferase

PDB id: 1w3d

Contents

Protein chain

46 a.a. *

* Residue conservation analysis

PDB id:

1w3d

Name:

Transferase

Title:

Nmr structure of the peripheral-subunit binding domain of bacillus stearothermophilus e2p

Structure:

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase. Chain: a. Fragment: residues 118-170. Synonym: complex dihydropoamide acetyltransferase. Engineered: yes

Source:

Geobacillus stearothermophilus. Organism_taxid: 1422. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Expression_system_variant: c41.

NMR struc:

20 models

Authors:

M.D.Allen,R.W.Broadhurst,R.G.Solomon,R.N.Perham

Key ref:

M.D.Allen et al. (2005). Interaction of the E2 and E3 components of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus. Use of a truncated protein domain in NMR spectroscopy. FEBS J, 272, 259-268. PubMed id: 15634348 DOI: 10.1111/j.1432-1033.2004.04405.x

Date:

14-Jul-04 Release date: 20-Jul-04

Protein chain

P11961  (ODP2_GEOSE) -  Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex from Geobacillus stearothermophilus

Seq: 428 a.a.

Struc: 46 a.a.

Enzyme reactions

• Enzyme class: E.C.2.3.1.12 - dihydrolipoyllysine-residue acetyltransferase.
• Pathway: Oxo-acid dehydrogenase complexes
• Reaction: N₆-[(R)-dihydrolipoyl]-L-lysyl-[protein] + acetyl-CoA = N₆-[(R)-S(8)- acetyldihydrolipoyl]-L-lysyl-[protein] + CoA

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

Added reference

DOI no: 10.1111/j.1432-1033.2004.04405.x

FEBS J 272:259-268 (2005)

PubMed id: 15634348

Interaction of the E2 and E3 components of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus. Use of a truncated protein domain in NMR spectroscopy.

M.D.Allen, R.W.Broadhurst, R.G.Solomon, R.N.Perham.

ABSTRACT

A (15)N-labelled peripheral-subunit binding domain (PSBD) of the dihydrolipoyl acetyltransferase (E2p) and the dimer of a solubilized interface domain (E3int) derived from the dihydrolipoyl dehydrogenase (E3) were used to investigate the basis of the interaction of E2p with E3 in the assembly of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus. Thirteen of the 55 amino acids in the PSBD show significant changes in either or both of the (15)N and (1)H amide chemical shifts when the PSBD forms a 1 : 1 complex with E3int. All of the 13 amino acids reside near the N-terminus of helix I of PSBD or in the loop region between helix II and helix III. (15)N backbone dynamics experiments on PSBD indicate that the structured region extends from Val129 to Ala168, with limited structure present in residues Asn126 to Arg128. The presence of structure in the region before helix I was confirmed by a refinement of the NMR structure of uncomplexed PSBD. Comparison of the crystal structure of the PSBD bound to E3 with the solution structure of uncomplexed PSBD described here indicates that the PSBD undergoes almost no conformational change upon binding to E3. These studies exemplify and validate the novel use of a solubilized, truncated protein domain in overcoming the limitations of high molecular mass on NMR spectroscopy.

Selected figure(s)

Figure 2.
Fig. 2. Backbone dynamics of PSBD. Plot of the backbone steady state {^1H}-^15N NOE enhancement, , for PSBD as a function of residue number.

Figure 3.
Fig. 3. Solution structure of PSBD from NMR spectroscopy. Superposition of backbone traces of the 25 accepted structures over residues 129–168, and a MOLSCRIPT[46] representation of the PSBD structure in the same orientation. The residues defining the secondary structural elements are labeled.

The above figures are reprinted by permission from the Federation of European Biochemical Societies: FEBS J (2005, 272, 259-268) copyright 2005.

Figures were selected by an automated process.