1JCC
Crystal Structure of a Novel Alanine-Zipper Trimer at 1.7 A Resolution, V13A,L16A,V20A,L23A,V27A,M30A,V34A mutations
Summary for 1JCC
Entry DOI | 10.2210/pdb1jcc/pdb |
Related | 1EQ7 1JCB 1JCD |
Descriptor | MAJOR OUTER MEMBRANE LIPOPROTEIN, ZINC ION (3 entities in total) |
Functional Keywords | lipoprotein, protein folding, coiled coil, helix capping, alanine-zipper, membrane protein |
Biological source | Escherichia coli |
Cellular location | Cell outer membrane ; Lipid-anchor : P69776 |
Total number of polymer chains | 3 |
Total formula weight | 17911.93 |
Authors | |
Primary citation | Liu, J.,Dai, J.,Lu, M. Zinc-Mediated Helix Capping in A Triple-Helical Protein Biochemistry, 42:5657-5664, 2003 Cited by PubMed Abstract: Specific sequence signals at alpha-helix termini can assist protein folding by punctuating and cueing secondary structural elements in the final native conformation. Here we report the crystallization of a 56-residue alanine-containing peptide, denoted Ala-10(56), in the presence of Zn(2+). The 1.7 A crystal structure shows that Ala-10(56) forms a parallel trimeric coiled coil with three zinc ions anchoring distinct capping conformations at the amino-terminal ends of the three helices. In each polypeptide chain, the free alpha-amino nitrogen and carbonyl oxygen of the amino-terminal Ser residue coordinate to a Zn(2+) ion to form a five-membered chelate, and the syn-unidentate interaction of the Asp7 side chain with the Zn(2+) cation leads to the formation of a unique docking arrangement for helix capping. Moreover, the coordination of the zinc ion involves a neighboring trimer molecule in the crystal. Consequently, the crystal contacts are stabilized by carboxylate-Zn(2+) interactions between four Ala-10(56) trimers in the crystal lattice. The observed synergy between the protein-zinc ion recognition and the helix-packing arrangements would contribute to the conformational specificity of the Ala-10(56) trimer. PubMed: 12741822DOI: 10.1021/bi026828a PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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