4XFW

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

4XFW の概要

• エントリーDOI: 10.2210/pdb4xfw/pdb
• 分子名称: Alpha-carbonic anhydrase, ZINC ION, CHLORIDE ION, ... (6 entities in total)
• 機能のキーワード: helicobacter pylori, carbonic anhydrase, metallo proteins, lyase
• 由来する生物種: Helicobacter pylori G27
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 52781.40

構造登録者

Compostella, M.E.,Vallese, F.,Berto, P.,Zanotti, G. (登録日: 2014-12-29, 公開日: 2015-08-05, 最終更新日: 2024-10-16)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.517 Å)