3R7C

The structure of a hexahestidine-tagged form of augmenter of liver regeneration reveals a novel Cd(2)Cl(4)O(6) cluster that aids in crystal packing

Summary for 3R7C

• Entry DOI: 10.2210/pdb3r7c/pdb
• Related: 1OQC
• Descriptor: FAD-linked sulfhydryl oxidase ALR, FLAVIN-ADENINE DINUCLEOTIDE, CHLORIDE ION, ... (6 entities in total)
• Functional Keywords: novel cd(2)cl(4)o(6) cluster, four-helical up-and-down bundle, all-helical fad binding motif, fad-linked sulfhydryl oxidase, liver regeneration, fad binding, mitochondrial intermembrane space, oxidoreductase
• Biological source: Rattus norvegicus (rat)
• Cellular location: Cytoplasm: Q63042
• Total number of polymer chains: 4
• Total formula weight: 70701.02

Authors

Florence, Q.J.,Wu, C.-K.,Swindell II, J.T.,Wang, B.C.,Rose, J.P. (deposition date: 2011-03-22, release date: 2012-03-28, Last modification date: 2025-11-12)

Primary citation

Florence, Q.,Wu, C.K.,Habel, J.,Swindell 2nd, J.T.,Wang, B.C.,Rose, J.P.
The structure of augmenter of liver regeneration crystallized in the presence of 50 mM CdCl2 reveals a novel Cd2Cl4O6 cluster that aids in crystal packing.
Acta Crystallogr.,Sect.D, 68:1128-1133, 2012

PubMed Abstract: 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).

PubMed: 22948913
DOI: 10.1107/S0907444912022561

Experimental method

X-RAY DIFFRACTION (2.4 Å)