PDBsum entry 2ip2

Transferase

PDB id: 2ip2

Contents

Protein chains

330 a.a. *

Waters ×512

* Residue conservation analysis

PDB id:

2ip2

Name:

Transferase

Title:

Structure of the pyocyanin biosynthetic protein phzm

Structure:

Probable phenazine-specific methyltransferase. Chain: a, b. Synonym: pyocyanin biosynthetic protein. Engineered: yes

Source:

Pseudomonas aeruginosa. Organism_taxid: 208964. Strain: pao1. Gene: phzm. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Dimer (from PQS)

Resolution:

1.80Å R-factor: 0.196 R-free: 0.247

Authors:

J.E.Ladner,J.F.Parsons,H.Robinson,K.Shi

Key ref:

J.F.Parsons et al. (2007). Structural and functional analysis of the pyocyanin biosynthetic protein PhzM from Pseudomonas aeruginosa. Biochemistry, 46, 1821-1828. PubMed id: 17253782

Date:

11-Oct-06 Release date: 24-Oct-06

Protein chains

Q9HWH2  (PHZM_PSEAE) -  Phenazine-1-carboxylate N-methyltransferase from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)

Seq: 334 a.a.

Struc: 330 a.a.

Enzyme reactions

• Enzyme class: E.C.2.1.1.327 - phenazine-1-carboxylate N-methyltransferase.
• Reaction: phenazine-1-carboxylate + S-adenosyl-L-methionine = 5-methyl-phenazine-1- carboxylate + S-adenosyl-L-homocysteine

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

Added reference

Biochemistry 46:1821-1828 (2007)

PubMed id: 17253782

Structural and functional analysis of the pyocyanin biosynthetic protein PhzM from Pseudomonas aeruginosa.

J.F.Parsons, B.T.Greenhagen, K.Shi, K.Calabrese, H.Robinson, J.E.Ladner.

ABSTRACT

Pyocyanin is a biologically active phenazine produced by the human pathogen Pseudomonas aeruginosa. It is thought to endow P. aeruginosa with a competitive growth advantage in colonized tissue and is also thought to be a virulence factor in diseases such as cystic fibrosis and AIDS where patients are commonly infected by pathogenic Pseudomonads due to their immunocompromised state. Pyocyanin is also a chemically interesting compound due to its unusual oxidation-reduction activity. Phenazine-1-carboxylic acid, the precursor to the bioactive phenazines, is synthesized from chorismic acid by enzymes encoded in a seven-gene cistron in P. aeruginosa and in other Pseudomonads. Phenzine-1-carboxylic acid is believed to be converted to pyocyanin by the sequential actions of the putative S-adenosylmethionine-dependent N-methyltransferase PhzM and the putative flavin-dependent hydroxylase PhzS. Here we report the 1.8 A crystal structure of PhzM determined by single anomalous dispersion. Unlike many methyltransferases, PhzM is a dimer in solution. The 36 kDa PhzM polypeptide folds into three domains. The C-terminal domain exhibits the alpha/beta-hydrolase fold typical of small molecule methyltransferases. Two smaller N-terminal domains form much of the dimer interface. Structural alignments with known methyltransferases show that PhzM is most similar to the plant O-methyltransferases that are characterized by an unusual intertwined dimer interface. The structure of PhzM contains no ligands, and the active site is open and solvent-exposed when compared to structures of similar enzymes. In vitro experiments using purified PhzM alone demonstrate that it has little or no ability to methylate phenzine-1-carboxylic acid. However, when the putative hydroxylase PhzS is included, pyocyanin is readily produced. This observation suggests that a mechanism has evolved in P. aeruginosa that ensures efficient production of pyocyanin via the prevention of the formation and release of an unstable and potentially deleterious intermediate.