1CPX

BETA FORM OF CARBOXYPEPTIDASE A (RESIDUES 3-307) FROM BOVINE PANCREAS IN AN ORTHORHOMBIC CRYSTAL FORM WITH TWO ZINC IONS IN THE ACTIVE SITE.

1CPX の概要

• エントリーDOI: 10.2210/pdb1cpx/pdb
• 分子名称: PROTEIN (CARBOXYPEPTIDASE A), ZINC ION, HYDROXIDE ION, ... (4 entities in total)
• 機能のキーワード: metalloprotease, hydrolase, carboxypeptidase, zinc inhibition, induced fit
• 由来する生物種: Bos taurus (cattle)
• 細胞内の位置: Secreted, extracellular space: P00730
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34593.24

構造登録者

Bukrinsky, J.T.,Bjerrum, M.J.,Kadziola, A. (登録日: 1998-07-27, 公開日: 1998-08-05, 最終更新日: 2024-11-20)

主引用文献

Bukrinsky, J.T.,Bjerrum, M.J.,Kadziola, A.
Native carboxypeptidase A in a new crystal environment reveals a different conformation of the important tyrosine 248.
Biochemistry, 37:16555-16564, 1998

PubMed Abstract: Native carboxypeptidase A has been crystallized in a new crystal form, and the structure has been refined with X-ray data to 2.0 A resolution. In contrast to the previously published structure [Rees, D. C., Lewis, M., and Lipscomb, W. N. (1983) J. Mol. Biol. 168, 367-387], no active-site amino acids are involved in the crystal packing. The important Tyr248 is stabilized inside the active site by a hydrogen bond and by interactions with Ile247. The proposed role of Tyr248 in the induced fit mechanism is therefore not supported by the findings in this structure of native carboxypeptidase A. The structure has a partly populated inhibitory Zn2+ site in close proximity to the catalytic Zn2+ as evident from X-ray anomalous dispersion data. A hydroxo bridge is found between the catalytic Zn2+ and the inhibitory Zn2+ with a Zn2+-Zn2+ distance of 3.48 A. In addition, the inhibitory Zn2+ has Glu270 as a monodentate ligand. No other protein ligands to the inhibitory Zn2+ are seen. The crystals were grown at 0.3 M LiCl and weak evidence for a binding site for partly competitive inhibitory anions is observed.

PubMed: 9843422
DOI: 10.1021/bi981678i

実験手法

X-RAY DIFFRACTION (2 Å)