Crystal structure of Escherichia coli L-asparaginase, an enzyme used in cancer therapy
Authors:
- A.L. Swain,
- Mariusz Jaskólski,
- D. Housset,
- J.K.M. Rao,
- A. Wlodawer
Abstract
The crystal structure of Escherichia coli asparaginase II (EC 3.5.1.1), a drug (Elspar) used for the treatment of acute lymphoblastic leukemia, has been determined at 2.3 Å resolution by using data from a single heavy atom derivative in combination with molecular replacement. The atomic model was refined to an R factor of 0.143. This enzyme, active as a homotetramer with 222 symmetry, belongs to the class of α/β proteins. Each subunit has two domains with unique topological features. On the basis of present structural evidence consistent with previous biochemical studies, we propose locations for the active sites between the N- and C-terminal domains belonging to different subunits and postulate a catalytic role for Thr-89.
- Record ID
- UAMed9f6ffef7bf4fb78ee642fba329e0f9
- Author
- Journal series
- Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424
- Issue year
- 1993
- Vol
- 90
- Pages
- 1474-1478
- ASJC Classification
- DOI
- DOI:10.1073/pnas.90.4.1474 opening in a new tab
- Language
- en English
- Score (nominal)
- 45
- Score source
- journalList
- Publication indicators
- = 213.000; : 2014 = 2.725; : 2006 = 9.643 (2) - 2007=10.369 (5)
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- Uniform Resource Identifier
- https://researchportal.amu.edu.pl/info/article/UAMed9f6ffef7bf4fb78ee642fba329e0f9/
* presented citation count is obtained through Internet information analysis and it is close to the number calculated by the Publish or Perishopening in a new tab system.
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