1t8z
From Proteopedia
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Atomic Structure of A Novel Tryptophan-Zipper Pentamer
Overview
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.
About this Structure
1T8Z is a Single protein structure of sequence from Escherichia coli with SO4 and 12P as ligands. Full crystallographic information is available from OCA.
Reference
Atomic structure of a tryptophan-zipper pentamer., Liu J, Yong W, Deng Y, Kallenbach NR, Lu M, Proc Natl Acad Sci U S A. 2004 Nov 16;101(46):16156-61. Epub 2004 Nov 1. PMID:15520380
Page seeded by OCA on Wed Nov 21 03:05:12 2007
Categories: Escherichia coli | Single protein | Deng, Y. | Kallenbach, N.R. | Liu, J. | Lu, M. | Yong, W. | 12P | SO4 | Coiled coil | Lipoprotein | Pentamer | Protein folding | Tryptophan-zipper
