1nns

L-asparaginase of E. coli in C2 space group and 1.95 A resolution

spinqualitylabelsall models 1nns, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1nns is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.95Å Ligands: ASP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ASPG2_ECOLI Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The functional L-asparaginase from Escherichia coli is a homotetramer with a molecular weight of about 142 kDa. The X-ray structure of the enzyme, crystallized in a new form (space group C2) and refined to 1.95 A resolution, is compared with that of the previously determined crystal form (space group P2(1)). The asymmetric unit of the new crystal form contains an L-asparaginase dimer instead of the tetramer found in the previous crystal form. It is found that crystal contacts practically do not affect the conformation of the protein. It is shown that subunit C of the tetrameric form is in a conformation which is systematically different from that of all other subunits in both crystal forms. Major conformational differences are confined to the lid loop (residues 14-27). In addition, the stability of this globular protein is analyzed in terms of the interactions between hydrophobic parts of the subunits. Structural comparison of Escherichia coli L-asparaginase in two monoclinic space groups.,Sanches M, Barbosa JA, de Oliveira RT, Abrahao Neto J, Polikarpov I Acta Crystallogr D Biol Crystallogr. 2003 Mar;59(Pt 3):416-22. Epub 2003, Feb 21. PMID:12595697 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Asparaginase 3D structures

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