1t8z
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1t8z.jpg|left|200px]] | [[Image:1t8z.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1t8z", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_1t8z| PDB=1t8z | SCENE= }} | |
| - | | | + | |
| - | + | ||
| - | }} | + | |
'''Atomic Structure of A Novel Tryptophan-Zipper Pentamer''' | '''Atomic Structure of A Novel Tryptophan-Zipper Pentamer''' | ||
| Line 30: | Line 27: | ||
[[Category: Lu, M.]] | [[Category: Lu, M.]] | ||
[[Category: Yong, W.]] | [[Category: Yong, W.]] | ||
| - | [[Category: | + | [[Category: Coiled coil]] |
| - | [[Category: | + | [[Category: Lipoprotein]] |
| - | [[Category: | + | [[Category: Pentamer]] |
| - | [[Category: | + | [[Category: Protein folding]] |
| - | [[Category: | + | [[Category: Tryptophan-zipper]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:41:11 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 06:41, 3 May 2008
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 Sat May 3 09:41:11 2008
