6YJN

Crystal structure of beta carbonic anhydrase from the pathogenic bacterium Burkholderia pseudomallei.

Summary for 6YJN

• Entry DOI: 10.2210/pdb6yjn/pdb
• Descriptor: Beta carbonic anhydrase, ZINC ION (3 entities in total)
• Functional Keywords: beta carbonic anhydrase, burkholderia pseudomallei, lyase
• Biological source: Burkholderia pseudomallei
• Total number of polymer chains: 1
• Total formula weight: 28334.42

Authors

Angeli, A.,Ferraroni, M. (deposition date: 2020-04-03, release date: 2020-06-10, Last modification date: 2024-01-24)

Primary citation

Angeli, A.,Ferraroni, M.,Pinteala, M.,Maier, S.S.,Simionescu, B.C.,Carta, F.,Del Prete, S.,Capasso, C.,Supuran, C.T.
Crystal Structure of a Tetrameric Type II beta-Carbonic Anhydrase from the Pathogenic BacteriumBurkholderia pseudomallei.
Molecules, 25:-, 2020

PubMed Abstract: Carbonic anhydrase (CA) is a zinc enzyme that catalyzes the reversible conversion of carbon dioxide to bicarbonate and proton. Currently, CA inhibitors are widely used as antiglaucoma, anticancer, and anti-obesity drugs and for the treatment of neurological disorders. Recently, the potential use of CA inhibitors to fight infections caused by protozoa, fungi, and bacteria has emerged as a new research line. In this article, the X-ray crystal structure of β-CA from was reported. The X-ray crystal structure of this new enzyme was solved at 2.7 Å resolution, revealing a tetrameric type II β-CA with a "closed" active site in which the zinc is tetrahedrally coordinated to Cys46, Asp48, His102, and Cys105. is known to encode at least two CAs, a β-CA, and a γ-CA. These proteins, playing a pivotal role in its life cycle and pathogenicity, offer a novel therapeutic opportunity to obtain antibiotics with a different mechanism of action. Furthermore, the new structure can provide a clear view of the β-CA mechanism of action and the possibility to find selective inhibitors for this class of CAs.

PubMed: 32408533
DOI: 10.3390/molecules25102269

Experimental method

X-RAY DIFFRACTION (2.7 Å)