1arm › Citations

Carboxypeptidase A: native, zinc-removed and mercury-replaced forms.

Greenblatt HM, Feinberg H, Tucker PA, Shoham G
Acta Crystallogr D Biol Crystallogr 54 289-305 (1998)
Related entries: 1arl, 1yme

Cited: 9 times
EuropePMC logo PMID: 9867434

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 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 chi2 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 citation agrees with previous proposals for the binding side of inhibitory zinc. These observations may explain some of the differences in kinetics observed in metal- replaced CPA.

Articles - 1arm mentioned but not cited (3)

  1. Peptide-plane flipping in proteins. Hayward S. Protein Sci. 10 2219-2227 (2001)
  2. De novo design of obligate ABC-type heterotrimeric proteins. Bermeo S, Favor A, Chang YT, Norris A, Boyken SE, Hsia Y, Haddox HK, Xu C, Brunette TJ, Wysocki VH, Bhabha G, Ekiert DC, Baker D. Nat Struct Mol Biol 29 1266-1276 (2022)
  3. Ligand-Binding-Site Refinement to Generate Reliable Holo Protein Structure Conformations from Apo Structures. Guterres H, Park SJ, Jiang W, Im W. J Chem Inf Model 61 535-546 (2021)


Articles citing this publication (6)

  1. Identifying cysteines and histidines in transition-metal-binding sites using support vector machines and neural networks. Passerini A, Punta M, Ceroni A, Rost B, Frasconi P. Proteins 65 305-316 (2006)
  2. Flexibility of metal binding sites in proteins on a database scale. Babor M, Greenblatt HM, Edelman M, Sobolev V. Proteins 59 221-230 (2005)
  3. Identification of the zinc binding ligands and the catalytic residue in human aspartoacylase, an enzyme involved in Canavan disease. Herga S, Berrin JG, Perrier J, Puigserver A, Giardina T. FEBS Lett. 580 5899-5904 (2006)
  4. High metal substitution tolerance of anthrax lethal factor and characterization of its active copper-substituted analogue. Lo SY, Säbel CE, Webb MI, Walsby CJ, Siemann S. J. Inorg. Biochem. 140 12-22 (2014)
  5. Molecular orbital study of complexes of zinc(II) with sulphide, thiomethanolate, thiomethanol, dimethylthioether, thiophenolate, formiate, acetate, carbonate, hydrogen carbonate, iminomethane and imidazole. Relationships with structural and catalytic zinc in some metallo-enzymes. Cini R. J. Biomol. Struct. Dyn. 16 1225-1237 (1999)
  6. Heteroleptic Coordination Environments in Metal-Mediated DNA G-Quadruplexes. Punt PM, Stratmann LM, Sevim S, Knauer L, Strohmann C, Clever GH. Front Chem 8 26 (2020)


Quick links