1t8z
From Proteopedia
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| , resolution 1.45Å | |||||||
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| Ligands: | , | ||||||
| Gene: | LPP, MLPA, MULI, B1677, C2072, Z2705, ECS2384, SF1706, S1839 (Escherichia coli) | ||||||
| Related: | 1eq7
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Sun Mar 30 23:53:02 2008
