This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1o7j
From Proteopedia
|
ATOMIC RESOLUTION STRUCTURE OF ERWINIA CHRYSANTHEMI L-ASPARAGINASE
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 ... [(full description)]
About this Structure
1O7J is a [Single protein] structure of sequence from [Erwinia chrysanthemi] with SO4, EDO and GOL as [ligands]. Active as [[1]], with EC number [3.5.1.1]. Full crystallographic information is available from [OCA].
Reference
Atomic resolution structure of Erwinia chrysanthemi L-asparaginase., Lubkowski J, Dauter M, Aghaiypour K, Wlodawer A, Dauter Z, Acta Crystallogr D Biol Crystallogr. 2003 Jan;59(Pt 1):84-92. Epub 2002, Dec 19. PMID:12499544
Page seeded by OCA on Mon Oct 29 21:31:32 2007
Categories: Erwinia chrysanthemi | Single protein | Aghaiypour, K. | Dauter, M. | Dauter, Z. | Lubkowski, J. | Wlodawer, A. | EDO | GOL | SO4 | Atomic resolution | Hydrolase | L-asparaginase
