1t8z

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|PDB= 1t8z |SIZE=350|CAPTION= <scene name='initialview01'>1t8z</scene>, resolution 1.45&Aring;
|PDB= 1t8z |SIZE=350|CAPTION= <scene name='initialview01'>1t8z</scene>, resolution 1.45&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=12P:DODECAETHYLENE GLYCOL'>12P</scene>
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|LIGAND= <scene name='pdbligand=12P:DODECAETHYLENE+GLYCOL'>12P</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
|ACTIVITY=
|ACTIVITY=
|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])
|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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|DOMAIN=
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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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[[Category: Lu, M.]]
[[Category: Lu, M.]]
[[Category: Yong, W.]]
[[Category: Yong, W.]]
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[[Category: 12P]]
 
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[[Category: SO4]]
 
[[Category: coiled coil]]
[[Category: coiled coil]]
[[Category: lipoprotein]]
[[Category: lipoprotein]]
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[[Category: tryptophan-zipper]]
[[Category: tryptophan-zipper]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:15:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:53:02 2008''

Revision as of 20:53, 30 March 2008


PDB ID 1t8z

Drag the structure with the mouse to rotate
, resolution 1.45Å
Ligands: ,
Gene: LPP, MLPA, MULI, B1677, C2072, Z2705, ECS2384, SF1706, S1839 (Escherichia coli)
Related: 1eq7


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

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