PDBsum entry 3pvr

Oxidoreductase

PDB id: 3pvr

Contents

Protein chains

304 a.a. *

236 a.a. *

248 a.a. *

Ligands

BYC

GOL ×7

Waters ×415

* Residue conservation analysis

PDB id:

3pvr

Name:

Oxidoreductase

Title:

The phenylacetyl-coa monooxygenase paaac subcomplex with benzoyl-coa

Structure:

Phenylacetic acid degradation protein paaa. Chain: a. Synonym: phenylacetyl-coa ring 1,2-epoxidase paaa. Engineered: yes. Phenylacetic acid degradation protein paac. Chain: b, c. Synonym: phenylacetyl-coa ring 1,2-epoxidase paac. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 511145. Strain: k12 substr. Mg1655. Gene: b1388, jw1383, paaa, ydbo. Expressed in: escherichia coli. Expression_system_taxid: 469008. Gene: b1390, jw1385, paac, ydbp.

Resolution:

2.10Å R-factor: 0.190 R-free: 0.225

Authors:

M.Cygler,A.M.Grishin,Montreal-Kingston Bacterial Structural Genomics Initiative (Bsgi)

Key ref:

A.M.Grishin et al. (2011). Structural and functional studies of the Escherichia coli phenylacetyl-CoA monooxygenase complex. J Biol Chem, 286, 10735-10743. PubMed id: 21247899 DOI: 10.1074/jbc.M110.194423

Date:

07-Dec-10 Release date: 19-Jan-11

Protein chain

P76077  (PAAA_ECOLI) -  1,2-phenylacetyl-CoA epoxidase, subunit A from Escherichia coli (strain K12)

Seq: 309 a.a.

Struc: 304 a.a.*

Protein chain

P76079  (PAAC_ECOLI) -  1,2-phenylacetyl-CoA epoxidase, subunit C from Escherichia coli (strain K12)

Seq: 248 a.a.

Struc: 236 a.a.*

Protein chain

P76079  (PAAC_ECOLI) -  1,2-phenylacetyl-CoA epoxidase, subunit C from Escherichia coli (strain K12)

Seq: 248 a.a.

Struc: 248 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

Enzyme reactions

• Enzyme class: Chain A: E.C.1.14.13.149 - phenylacetyl-CoA 1,2-epoxidase.
• Reaction: phenylacetyl-CoA + NADPH + O2 + H⁺ = 2-(1,2-epoxy-1,2- dihydrophenyl)acetyl-CoA + NADP⁺ + H2O

phenylacetyl-CoA + NADPH + O2 + H(+) (Bound ligand (Het Group name = BYC) matches with 98.25% similarity) = 2-(1,2-epoxy-1,2- dihydrophenyl)acetyl-CoA + NADP(+) + H2O

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

reference

DOI no: 10.1074/jbc.M110.194423

J Biol Chem 286:10735-10743 (2011)

PubMed id: 21247899

Structural and functional studies of the Escherichia coli phenylacetyl-CoA monooxygenase complex.

A.M.Grishin, E.Ajamian, L.Tao, L.Zhang, R.Menard, M.Cygler.

ABSTRACT

The utilization of phenylacetic acid (PA) in Escherichia coli occurs through a hybrid pathway that shows features of both aerobic and anaerobic metabolism. Oxygenation of the aromatic ring is performed by a multisubunit phenylacetyl-coenzyme A oxygenase complex that shares remote homology of two subunits to well studied bacterial multicomponent monooxygenases and was postulated to form a new bacterial multicomponent monooxygenase subfamily. We expressed the subunits PaaA, B, C, D, and E of the PA-CoA oxygenase and showed that PaaABC, PaaAC, and PaaBC form stable subcomplexes that can be purified. In vitro reconstitution of the oxygenase subunits showed that each of the PaaA, B, C, and E subunits are necessary for catalysis, whereas PaaD is not essential. We have determined the crystal structure of the PaaAC complex in a ligand-free form and with several CoA derivatives. We conclude that PaaAC forms a catalytic core with a monooxygenase fold with PaaA being the catalytic α subunit and PaaC, the structural β subunit. PaaAC forms heterotetramers that are organized very differently from other known multisubunit monooxygenases and lacks their conservative network of hydrogen bonds between the di-iron center and protein surface, suggesting different association with the reductase and different mechanisms of electron transport. The PaaA structure shows adaptation of the common access route to the active site for binding a CoA-bound substrate. The enzyme-substrate complex shows the orientation of the aromatic ring, which is poised for oxygenation at the ortho-position, in accordance with the expected chemistry. The PA-CoA oxygenase complex serves as a paradigm for the new subfamily multicomponent monooxygenases comprising several hundred homologs.