Carboxypeptidase A: Native, zinc-removed and mercury-replaced forms

H. M. Greenblatt, H. Feinberg, P. A. Tucker, G. Shoham

Research output: Contribution to journalArticlepeer-review

30 Scopus citations

Abstract

The crystal structure of the zinc-containing exopeptidase bovine carboxypeptidase A (CPA) has been refined to high resolution, based on a data set collected from a single crystal, incorporating new sequence information based on cloning of the bovine gene. In addition, new refined structures are available for the zinc-removed form of the enzyme, apo-CPA, as well as the mercury-replaced form, Hg-CPA. The native structure reveals that the zinc-bound water molecule does not appear to be more loosely bound than the rest of the zinc ligands, at least when B-factor values are considered. Nor is there any evidence for a secondary location of this water molecule. The apo-enzyme structure does not show any density in the place of the removed zinc ion. The only significant change appears to be a X2 rotation of one zinc histidine ligand to form an ion-pair interaction with a glutamic acid side chain. The structure of Hg-CPA reveals a solvent Tris molecule bound to the mercury cation, as well as an unidentified cation bound to Glu270. The location of this cation agrees with previous proposals for the binding site of inhibitory zinc. These observations may explain some of the differences in kinetics observed in metal-replaced CPA.

Original languageAmerican English
Pages (from-to)289-305
Number of pages17
JournalActa Crystallographica Section D: Biological Crystallography
Volume54
Issue number3
DOIs
StatePublished - 1998

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