1T8Z
Atomic Structure of A Novel Tryptophan-Zipper Pentamer
Summary for 1T8Z
Entry DOI | 10.2210/pdb1t8z/pdb |
Related | 1eq7 |
Descriptor | Major outer membrane lipoprotein, SULFATE ION, DODECAETHYLENE GLYCOL, ... (4 entities in total) |
Functional Keywords | lipoprotein, protein folding, coiled coil, pentamer, tryptophan-zipper, membrane protein |
Biological source | Escherichia coli |
Cellular location | Cell outer membrane; Lipid-anchor: P69776 |
Total number of polymer chains | 5 |
Total formula weight | 35144.66 |
Authors | Liu, J.,Yong, W.,Deng, Y.,Kallenbach, N.R.,Lu, M. (deposition date: 2004-05-13, release date: 2004-11-23, Last modification date: 2024-02-14) |
Primary citation | Liu, J.,Yong, W.,Deng, Y.,Kallenbach, N.R.,Lu, M. Atomic structure of a tryptophan-zipper pentamer. Proc.Natl.Acad.Sci.USA, 101:16156-16161, 2004 Cited by PubMed Abstract: Coiled-coil motifs are ubiquitous mediators of specific protein-protein interactions through the formation of interlocking hydrophobic seams between alpha-helical chains. Residues that form these seams occur at the first (a) and fourth (d) positions of a characteristic 7-aa repeat and are primarily aliphatic. The potential of aromatic residues to promote helix association in a coiled coil was explored by engineering a "Trp-zipper" protein with Trp residues at all 14 a and d positions. The protein forms a discrete, stable, alpha-helical pentamer in water at physiological pH. Its 1.45-A crystal structure reveals a parallel, five-stranded coiled coil, a previously uncharacterized type of "knobs-into-holes" packing interaction between interfacial Trp side chains, and an unusual approximately 8-A-diameter axial channel lined with indole rings that is filled with polyethylene glycol 400 and water and sulfate ion molecules. The engineered Trp-zipper pentamer enlarges current views of coiled-coil assembly, molecular recognition, and protein engineering, and may serve as a soluble model for membrane ion channels. PubMed: 15520380DOI: 10.1073/pnas.0405319101 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.45 Å) |
Structure validation
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