Crystal structure of human erythrocyte carbonic anhydrase B. Three-dimensional structure at a nominal 2.2-A resolution - PubMed (original) (raw)

Crystal structure of human erythrocyte carbonic anhydrase B. Three-dimensional structure at a nominal 2.2-A resolution

K K Kannan et al. Proc Natl Acad Sci U S A. 1975 Jan.

Abstract

The three-dimensional structure of carbonic anhydrase B (EC 4,2,1,1; carbonate hydro-lyase) from human erythrocytes has been determined to high resolution. Parallel and antiparallel pleated sheet makes up the predominant secondary structure of the enzyme. The tertiary structure is unique for its folding and is very similar to the structure is unique for its folding and is very similar to the structure of the isoenzyme, human erythrocyte carbonic anhydrase C. The essential metal ion, zinc, is firmly bound to the enzyme through three histidyl ligands and located at the bottom of a 12-A deep conical cavity. The zinc ligands are involved in a number of hydrogen bond formations with residues in the immediate vicinity of the active site cavity. Some of the similarities and differences in the sidechain orientation and active site topography of the two isoenzymes are also discussed.

PubMed Disclaimer

Similar articles

Cited by

References

    1. J Physiol. 1933 Dec 5;80(2):113-42 - PubMed
    1. J Mol Biol. 1968 Oct 14;37(1):225-30 - PubMed
    1. Hoppe Seylers Z Physiol Chem. 1963;334:279-82 - PubMed
    1. Biochim Biophys Acta. 1961 Sep 2;52:1-12 - PubMed
    1. Nat New Biol. 1972 Feb 2;235(57):131-7 - PubMed

Publication types

MeSH terms

Substances

LinkOut - more resources