1jcc
From Proteopedia
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|PDB= 1jcc |SIZE=350|CAPTION= <scene name='initialview01'>1jcc</scene>, resolution 1.70Å | |PDB= 1jcc |SIZE=350|CAPTION= <scene name='initialview01'>1jcc</scene>, resolution 1.70Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1eq7|1EQ7]], [[1jcb|1JCB]], [[1jcd|1JCD]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jcc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jcc OCA], [http://www.ebi.ac.uk/pdbsum/1jcc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jcc RCSB]</span> | ||
}} | }} | ||
| Line 25: | Line 28: | ||
[[Category: Liu, J.]] | [[Category: Liu, J.]] | ||
[[Category: Lu, M.]] | [[Category: Lu, M.]] | ||
| - | [[Category: ZN]] | ||
[[Category: alanine-zipper]] | [[Category: alanine-zipper]] | ||
[[Category: coiled coil]] | [[Category: coiled coil]] | ||
| Line 32: | Line 34: | ||
[[Category: protein folding]] | [[Category: protein folding]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:31:41 2008'' |
Revision as of 18:31, 30 March 2008
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| , resolution 1.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Related: | 1EQ7, 1JCB, 1JCD
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of a Novel Alanine-Zipper Trimer at 1.7 A Resolution, V13A,L16A,V20A,L23A,V27A,M30A,V34A mutations
Overview
Specific sequence signals at alpha-helix termini can assist protein folding by punctuating and cueing secondary structural elements in the final native conformation. Here we report the crystallization of a 56-residue alanine-containing peptide, denoted Ala-10(56), in the presence of Zn(2+). The 1.7 A crystal structure shows that Ala-10(56) forms a parallel trimeric coiled coil with three zinc ions anchoring distinct capping conformations at the amino-terminal ends of the three helices. In each polypeptide chain, the free alpha-amino nitrogen and carbonyl oxygen of the amino-terminal Ser residue coordinate to a Zn(2+) ion to form a five-membered chelate, and the syn-unidentate interaction of the Asp7 side chain with the Zn(2+) cation leads to the formation of a unique docking arrangement for helix capping. Moreover, the coordination of the zinc ion involves a neighboring trimer molecule in the crystal. Consequently, the crystal contacts are stabilized by carboxylate-Zn(2+) interactions between four Ala-10(56) trimers in the crystal lattice. The observed synergy between the protein-zinc ion recognition and the helix-packing arrangements would contribute to the conformational specificity of the Ala-10(56) trimer.
About this Structure
1JCC is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Zinc-mediated helix capping in a triple-helical protein., Liu J, Dai J, Lu M, Biochemistry. 2003 May 20;42(19):5657-64. PMID:12741822
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