4XFW: Crystal Structure Of The Monoclinic Form Of Alpha-carbonic Anhydrase From The Human Pathogen Helicobacter Pylori

The crystal structure of alpha-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.
PDB ID: 4XFWDownload
MMDB ID: 131444
PDB Deposition Date: 2014/12/29
Updated in MMDB: 2015/08
Experimental Method:
x-ray diffraction
Resolution: 1.52  Å
Source Organism:
Similar Structures:
Biological Unit for 4XFW: dimeric; determined by author and by software (PISA)
Molecular Components in 4XFW
Label Count Molecule
Proteins (2 molecules)
Alpha-carbonic Anhydrase
Molecule annotation
Chemicals (6 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB