1EKJ

THE X-RAY CRYSTALLOGRAPHIC STRUCTURE OF BETA CARBONIC ANHYDRASE FROM THE C3 DICOT PISUM SATIVUM

1EKJ の概要

• エントリーDOI: 10.2210/pdb1ekj/pdb
• 分子名称: BETA-CARBONIC ANHYDRASE, ACETATE ION, AZIDE ION, ... (9 entities in total)
• 機能のキーワード: rossman fold domain, strand exchange, lyase
• 由来する生物種: Pisum sativum (pea)
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 193939.28

構造登録者

Kimber, M.S.,Pai, E.F. (登録日: 2000-03-08, 公開日: 2000-06-07, 最終更新日: 2024-02-07)

主引用文献

Kimber, M.S.,Pai, E.F.
The active site architecture of Pisum sativum beta-carbonic anhydrase is a mirror image of that of alpha-carbonic anhydrases.
EMBO J., 19:1407-1418, 2000

PubMed Abstract: We have determined the structure of the beta-carbonic anhydrase from the dicotyledonous plant Pisum sativum at 1.93 A resolution, using a combination of multiple anomalous scattering off the active site zinc ion and non-crystallographic symmetry averaging. The mol- ecule assembles as an octamer with a novel dimer of dimers of dimers arrangement. Two distinct patterns of conservation of active site residues are observed, implying two potentially mechanistically distinct classes of beta-carbonic anhydrases. The active site is located at the interface between two monomers, with Cys160, His220 and Cys223 binding the catalytic zinc ion and residues Asp162 (oriented by Arg164), Gly224, Gln151, Val184, Phe179 and Tyr205 interacting with the substrate analogue, acetic acid. The substrate binding groups have a one to one correspondence with the functional groups in the alpha-carbonic anhydrase active site, with the corresponding residues being closely superimposable by a mirror plane. Therefore, despite differing folds, alpha- and beta-carbonic anhydrase have converged upon a very similar active site design and are likely to share a common mechanism.

PubMed: 10747009
DOI: 10.1093/emboj/19.7.1407

実験手法

X-RAY DIFFRACTION (1.93 Å)