1O7J
Atomic resolution structure of Erwinia chrysanthemi L-asparaginase
Summary for 1O7J
| Entry DOI | 10.2210/pdb1o7j/pdb |
| Related | 1HFJ 1HFK 1HFW 1HG0 1HG1 1JSL 1JSR |
| Descriptor | L-ASPARAGINASE, SULFATE ION, GLYCEROL, ... (5 entities in total) |
| Functional Keywords | l-asparaginase, atomic resolution, hydrolase |
| Biological source | ERWINIA CHRYSANTHEMI |
| Total number of polymer chains | 4 |
| Total formula weight | 142189.59 |
| Authors | Lubkowski, J.,Dauter, M.,Aghaiypour, K.,Wlodawer, A.,Dauter, Z. (deposition date: 2002-11-07, release date: 2002-12-04, Last modification date: 2023-12-13) |
| Primary citation | Lubkowski, J.,Dauter, M.,Aghaiypour, K.,Wlodawer, A.,Dauter, Z. Atomic Resolution Structure of Erwinia Chrysanthemi L-Asparaginase Acta Crystallogr.,Sect.D, 59:84-, 2003 Cited by PubMed Abstract: An X-ray structure of L-asparaginase from Erwinia chrysanthemi (ErA) has been refined at 1 A resolution to an R factor of below 0.1, using data collected on a synchrotron source. With four molecules of the enzyme consisting of 327 amino acids each, this crystal contains one of the largest asymmetric units of a protein refined to date at atomic resolution. Previously, structures of ErA and of related enzymes from other bacterial sources have been refined at resolutions not exceeding 1.7 A; thus, the present structure represents a very significant improvement in the quality of the available models of these proteins and should provide a good basis for future studies of the conformational variability of proteins, identification of subtle conformational features and corroboration of the stereochemical libraries, amongst other things. L-Asparaginases, which are enzymes that catalyze the hydrolysis of L-asparagine to aspartic acid, have been used for over 30 y as therapeutic agents in the treatment of acute childhood lymphoblastic leukemia, although the details of the enzymatic reaction and substrate specificity have not yet been completely elucidated. This atomic resolution structure is a step in that direction. PubMed: 12499544DOI: 10.1107/S0907444902019443 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1 Å) |
Structure validation
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