1cpx
From Proteopedia
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BETA FORM OF CARBOXYPEPTIDASE A (RESIDUES 3-307) FROM BOVINE PANCREAS IN AN ORTHORHOMBIC CRYSTAL FORM WITH TWO ZINC IONS IN THE ACTIVE SITE.
Overview
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.
About this Structure
1CPX is a Single protein structure of sequence from Bos taurus with ZN and OH as ligands. Active as Carboxypeptidase A, with EC number 3.4.17.1 Full crystallographic information is available from OCA.
Reference
Native carboxypeptidase A in a new crystal environment reveals a different conformation of the important tyrosine 248., Bukrinsky JT, Bjerrum MJ, Kadziola A, Biochemistry. 1998 Nov 24;37(47):16555-64. PMID:9843422
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