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1t8z

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[[Image:1t8z.jpg|left|200px]]
[[Image:1t8z.jpg|left|200px]]
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{{Structure
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|PDB= 1t8z |SIZE=350|CAPTION= <scene name='initialview01'>1t8z</scene>, resolution 1.45&Aring;
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|GENE= LPP, MLPA, MULI, B1677, C2072, Z2705, ECS2384, SF1706, S1839 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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{{STRUCTURE_1t8z| PDB=1t8z | SCENE= }}
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|RELATEDENTRY=[[1eq7|1eq7]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1t8z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t8z OCA], [http://www.ebi.ac.uk/pdbsum/1t8z PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1t8z RCSB]</span>
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'''Atomic Structure of A Novel Tryptophan-Zipper Pentamer'''
'''Atomic Structure of A Novel Tryptophan-Zipper Pentamer'''
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[[Category: Lu, M.]]
[[Category: Lu, M.]]
[[Category: Yong, W.]]
[[Category: Yong, W.]]
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[[Category: coiled coil]]
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[[Category: Coiled coil]]
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[[Category: lipoprotein]]
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[[Category: Lipoprotein]]
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[[Category: pentamer]]
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[[Category: Pentamer]]
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[[Category: protein folding]]
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[[Category: Protein folding]]
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[[Category: tryptophan-zipper]]
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[[Category: Tryptophan-zipper]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:41:11 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:53:02 2008''
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Revision as of 06:41, 3 May 2008

Template:STRUCTURE 1t8z

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

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