PDBsum entry 4cs0

Lyase

PDB id: 4cs0

Contents

Protein chains

127 a.a.

127 a.a.

Ligands

SCN

ACO

Metals

_MG

Waters ×62

PDB id:

4cs0

Name:

Lyase

Title:

Direct visualisation of strain-induced protein post-translational modification

Structure:

Aspartate 1-decarboxylase. Chain: a. Synonym: aspartate alpha-decarboxylase. Engineered: yes. Mutation: yes. Panz. Chain: b. Engineered: yes

Source:

Escherichia coli k-12. Organism_taxid: 83333. Expressed in: escherichia coli k-12. Expression_system_taxid: 83333. Expression_system_variant: mg1655 pand-panz-(de3).

Resolution:

2.10Å R-factor: 0.175 R-free: 0.237

Authors:

D.C.F.Monteiro,V.Patel,C.P.Bartlett,T.D.Grant,S.Nozaki,J.A.Gowdy, E.H.Snell,H.Niki,A.R.Pearson,M.E.Webb

Key ref:

D.C.Monteiro et al. (2015). The structure of the PanD/PanZ protein complex reveals negative feedback regulation of pantothenate biosynthesis by coenzyme A. Chem Biol, 22, 492-503. PubMed id: 25910242 DOI: 10.1016/j.chembiol.2015.03.017

Date:

02-Mar-14 Release date: 25-Mar-15

Protein chain

P0A790  (PAND_ECOLI) -  Aspartate 1-decarboxylase from Escherichia coli (strain K12)

Seq: 126 a.a.

Struc: 127 a.a.*

Protein chain

P37613  (PANZ_ECOLI) -  PanD regulatory factor from Escherichia coli (strain K12)

Seq: 127 a.a.

Struc: 127 a.a.

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Enzyme reactions

• Enzyme class: Chain A: E.C.4.1.1.11 - aspartate 1-decarboxylase.
• Pathway: Coenzyme A Biosynthesis (early stages)
• Reaction: L-aspartate + H⁺ = beta-alanine + CO2
• Cofactor: Pyruvate

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

reference

DOI no: 10.1016/j.chembiol.2015.03.017

Chem Biol 22:492-503 (2015)

PubMed id: 25910242

The structure of the PanD/PanZ protein complex reveals negative feedback regulation of pantothenate biosynthesis by coenzyme A.

D.C.Monteiro, V.Patel, C.P.Bartlett, S.Nozaki, T.D.Grant, J.A.Gowdy, G.S.Thompson, A.P.Kalverda, E.H.Snell, H.Niki, A.R.Pearson, M.E.Webb.

ABSTRACT

Coenzyme A (CoA) is an ubiquitous and essential cofactor, synthesized from the precursor pantothenate. Vitamin biosynthetic pathways are normally tightly regulated, including the pathway from pantothenate to CoA. However, no regulation of pantothenate biosynthesis has been identified. We have recently described an additional component in the pantothenate biosynthetic pathway, PanZ, which promotes the activation of the zymogen, PanD, to form aspartate α-decarboxylase (ADC) in a CoA-dependent manner. Here we report the structure of PanZ in complex with PanD, which reveals the structural basis for the CoA dependence of this interaction and activation. In addition, we show that PanZ acts as a CoA-dependent inhibitor of ADC catalysis. This inhibitory effect can effectively regulate the biosynthetic pathway to pantothenate, and thereby also regulate CoA biosynthesis. This represents a previously unobserved mode of metabolic regulation whereby a cofactor-utilizing protein negatively regulates the biosynthesis of the same cofactor.