4XFW

Crystal structure of the monoclinic form of alpha-carbonic anhydrase from the human pathogen Helicobacter pylori

Summary for 4XFW

• Entry DOI: 10.2210/pdb4xfw/pdb
• Descriptor: Alpha-carbonic anhydrase, ZINC ION, CHLORIDE ION, ... (6 entities in total)
• Functional Keywords: helicobacter pylori, carbonic anhydrase, metallo proteins, lyase
• Biological source: Helicobacter pylori G27
• Total number of polymer chains: 2
• Total formula weight: 52781.40

Authors

Compostella, M.E.,Vallese, F.,Berto, P.,Zanotti, G. (deposition date: 2014-12-29, release date: 2015-08-05, Last modification date: 2024-10-16)

Primary citation

Compostella, M.E.,Berto, P.,Vallese, F.,Zanotti, G.
Structure of alpha-carbonic anhydrase from the human pathogen Helicobacter pylori.
Acta Crystallogr.,Sect.F, 71:1005-1011, 2015

PubMed Abstract: The crystal structure of α-carbonic anhydrase, an enzyme present in the periplasm of Helicobacter pylori, a bacterium that affects humans and that is responsible for several gastric pathologies, is described. Two enzyme monomers are present in the asymmetric unit of the monoclinic space group P21, forming a dimer in the crystal. Despite the similarity of the enzyme structure to those of orthologues from other species, the H. pylori protein has adopted peculiar features in order to allow the bacterium to survive in the difficult environment of the human stomach. In particular, the crystal structure shows how the bacterium has corrected for the mutation of an essential amino acid important for catalysis using a negative ion from the medium and how it localizes close to the inner membrane in the periplasm. Since carbonic anhydrase is essential for the bacterial colonization of the host, it is a potential target for antibiotic drugs. The definition of the shape of the active-site entrance and cavity constitutes a basis for the design of specific inhibitors.

PubMed: 26249690
DOI: 10.1107/S2053230X15010407

Experimental method

X-RAY DIFFRACTION (1.517 Å)