Kannan, K. K. ; Notstrand, B. ; Fridborg, K. ; Lovgren, S. ; Ohlsson, A. ; Petef, M. (1975) Crystal structure of human erythrocyte carbonic anhydrase B. Three-dimensional structure at a nominal 2.2-Å resolution Proceedings of the National Academy of Sciences of the United States of America, 72 (1). pp. 51-55. ISSN 0027-8424
|
PDF
- Publisher Version
1MB |
Official URL: http://www.pnas.org/content/72/1/51.abstract
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-Å 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.
Item Type: | Article |
---|---|
Source: | Copyright of this article belongs to National Academy of Sciences, USA. |
ID Code: | 19034 |
Deposited On: | 25 Nov 2010 14:34 |
Last Modified: | 17 May 2016 03:40 |
Repository Staff Only: item control page