| Autor: |
Florence Q; Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, USA., Wu CK, Habel J, Swindell JT 2nd, Wang BC, Rose JP |
| Jazyk: |
angličtina |
| Zdroj: |
Acta crystallographica. Section D, Biological crystallography [Acta Crystallogr D Biol Crystallogr] 2012 Sep; Vol. 68 (Pt 9), pp. 1128-33. Date of Electronic Publication: 2012 Aug 18. |
| DOI: |
10.1107/S0907444912022561 |
| Abstrakt: |
The crystal structure of the protein augmenter of liver regeneration containing a 14-residue hexahistidine purification tag (hsALR) has been determined to 2.4 Å resolution by Cd-SAD using a highly redundant data set collected on a rotating-anode home X-ray source and processed in 1998. The hsALR crystal structure is a tetramer composed of two homodimers bridged by a novel Cd(2)Cl(4)O(6) cluster via binding to the side-chain carboxylate groups of two solvent-exposed aspartic acid residues. A comparison with the native sALR tetramer shows that the cluster dramatically changes the hsALR dimer-dimer interface, which can now better accommodate the extra 14 N-terminal residues associated with the purification tag. The refined 2.4 Å resolution structure is in good agreement with both the X-ray data (R(cryst) of 0.165, R(free) of 0.211) and the expected stereochemistry (r.m.s. deviations from ideality for bond lengths and bond angles of 0.007 Å and 1.15°, respectively). |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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