PDBsum entry 6d2m

Lyase

PDB id: 6d2m

Contents

Protein chain

209 a.a.

Ligands

IMD ×2

Metals

_ZN

Waters ×65

PDB id:

6d2m

Name:

Lyase

Title:

Beta carbonic anhydrase in complex with thiocyanate

Structure:

Carbonic anhydrase. Chain: a. Synonym: carbonate dehydratase. Engineered: yes

Source:

Pseudomonas aeruginosa. Organism_taxid: 287. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.90Å R-factor: 0.180 R-free: 0.220

Authors:

A.Murray,M.Aggarwal,M.Pinard,R.Mckenna

Key ref:

A.B.Murray et al. (2018). Structural Mapping of Anion Inhibitors to β-Carbonic Anhydrase psCA3 from Pseudomonas aeruginosa. ChemMedChem, 13, 2024-2029. PubMed id: 30088334 DOI: 10.1002/cmdc.201800375

Date:

13-Apr-18 Release date: 05-Sep-18

Protein chain

Q9HVB9  (Q9HVB9_PSEAE) -  Carbonic anhydrase from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)

Seq: 215 a.a.

Struc: 209 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.4.2.1.1 - carbonic anhydrase.
• Reaction: hydrogencarbonate + H⁺ = CO2 + H2O
• Cofactor: Zn(2+)

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

Added reference

DOI no: 10.1002/cmdc.201800375

ChemMedChem 13:2024-2029 (2018)

PubMed id: 30088334

Structural Mapping of Anion Inhibitors to β-Carbonic Anhydrase psCA3 from Pseudomonas aeruginosa.

A.B.Murray, M.Aggarwal, M.Pinard, D.Vullo, M.Patrauchan, C.T.Supuran, R.McKenna.

ABSTRACT

Pseudomonas aeruginosa is a Gram-negative facultative anaerobe belonging to the Pseudomonadaceae family. It is a multidrug-resistant opportunistic human pathogen, a common cause of life-threatening nosocomial infections, and a key bacterial agent in cystic fibrosis and endocarditis. The bacterium exhibits intrinsic resistance to most antibacterial agents, including aminoglycosides and quinolones. Hence, the identification of new drug targets for P. aeruginosa is ongoing. PsCA3 is a β-class carbonic anhydrase (β-CA) that catalyzes the reversible hydration of carbon dioxide to bicarbonate and represents a new class of antimicrobial target. Previously, inhibitor screening studies of psCA3 have shown that a series of small anions including sulfamide (SFN), imidazole (IMD), and 4-methylimidazole (4MI), and thiocyanate (SCN) inhibit the enzyme with efficiencies in the micro- to millimolar range. Herein the X-ray crystal structures of these inhibitors in complex with psCA3 are presented and compared with human CA II. This structural survey into the binding modes of small anions forms the foundation for the development of inhibitors against β-CAs and more selective inhibitors against P. aeruginosa.