1o7j: Difference between revisions
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==Overview== | ==Overview== | ||
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 ... | 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. | ||
==About this Structure== | ==About this Structure== | ||
1O7J is a | 1O7J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Erwinia_chrysanthemi Erwinia chrysanthemi] with SO4, EDO and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Asparaginase Asparaginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.1 3.5.1.1] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1O7J OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: l-asparaginase]] | [[Category: l-asparaginase]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 15:12:22 2007'' | ||
