1t8z
From Proteopedia
(New page: 200px<br /><applet load="1t8z" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t8z, resolution 1.45Å" /> '''Atomic Structure of ...) |
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| - | [[Image:1t8z.jpg|left|200px]]<br /><applet load="1t8z" size=" | + | [[Image:1t8z.jpg|left|200px]]<br /><applet load="1t8z" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1t8z, resolution 1.45Å" /> | caption="1t8z, resolution 1.45Å" /> | ||
'''Atomic Structure of A Novel Tryptophan-Zipper Pentamer'''<br /> | '''Atomic Structure of A Novel Tryptophan-Zipper Pentamer'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Coiled-coil motifs are ubiquitous mediators of specific protein-protein | + | 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== | ==About this Structure== | ||
| - | 1T8Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4 and 12P as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1T8Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=12P:'>12P</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T8Z OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Deng, Y.]] | [[Category: Deng, Y.]] | ||
| - | [[Category: Kallenbach, N | + | [[Category: Kallenbach, N R.]] |
[[Category: Liu, J.]] | [[Category: Liu, J.]] | ||
[[Category: Lu, M.]] | [[Category: Lu, M.]] | ||
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[[Category: tryptophan-zipper]] | [[Category: tryptophan-zipper]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:11:09 2008'' |
Revision as of 13:11, 21 February 2008
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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 and 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 Thu Feb 21 15:11:09 2008
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
