3B1B

The unique structure of wild type carbonic anhydrase alpha-CA1 from Chlamydomonas reinhardtii

3B1B の概要

• エントリーDOI: 10.2210/pdb3b1b/pdb
• 分子名称: Carbonic anhydrase 1, ZINC ION, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: n-glycosylation, zinc-finger, carbonic anhydrase, lyase
• 由来する生物種: Chlamydomonas reinhardtii
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 84886.59

構造登録者

Shimizu, S.,Takenaka, A. (登録日: 2011-06-29, 公開日: 2011-11-16, 最終更新日: 2024-10-30)

主引用文献

Suzuki, K.,Yang, S.Y.,Shimizu, S.,Morishita, E.C.,Jiang, J.,Zhang, F.,Hoque, M.M.,Sato, Y.,Tsunoda, M.,Sekiguchi, T.,Takenaka, A.
The unique structure of carbonic anhydrase alpha CA1 from Chlamydomonas reinhardtii
Acta Crystallogr.,Sect.D, 67:894-901, 2011

PubMed Abstract: Chlamydomonas reinhardtii α-type carbonic anhydrase (Cr-αCA1) is a dimeric enzyme that catalyses the interconversion of carbon dioxide and carbonic acid. The precursor form of Cr-αCA1 undergoes post-translational cleavage and N-glycosylation. Comparison of the genomic sequences of precursor Cr-αCA1 and other αCAs shows that Cr-αCA1 contains a different N-terminal sequence and two insertion sequences. A 35-residue peptide in one of the insertion sequences is deleted from the precursor during maturation. The crystal structure of the mature form of Cr-αCA1 has been determined at 1.88 Å resolution. Each subunit is cleaved into the long and short peptides, but they are linked together by a disulfide bond. The two subunits are linked by a disulfide bond. N-Glycosylations occur at three asparagine residues and the attached N-glycans protrude into solvent regions. The subunits consist of a core β-sheet structure composed of nine β-strands. At the centre of the β-sheet is the catalytic site, which contains a Zn atom bound to three histidine residues. The amino-acid residues around the Zn atom are highly conserved in other monomeric and dimeric αCAs. The short peptide runs near the active site and forms a hydrogen bond to the zinc-coordinated residue in the long chain, suggesting an important role for the short peptide in Cr-αCA1 activity.

PubMed: 21931221
DOI: 10.1107/S0907444911032884

実験手法

X-RAY DIFFRACTION (1.88 Å)