1jcc

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[[Image:1jcc.gif|left|200px]]
[[Image:1jcc.gif|left|200px]]
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{{Structure
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|PDB= 1jcc |SIZE=350|CAPTION= <scene name='initialview01'>1jcc</scene>, resolution 1.70&Aring;
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The line below this paragraph, containing "STRUCTURE_1jcc", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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{{STRUCTURE_1jcc| PDB=1jcc | SCENE= }}
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|RELATEDENTRY=[[1eq7|1EQ7]], [[1jcb|1JCB]], [[1jcd|1JCD]]
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|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>
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'''Crystal Structure of a Novel Alanine-Zipper Trimer at 1.7 A Resolution, V13A,L16A,V20A,L23A,V27A,M30A,V34A mutations'''
'''Crystal Structure of a Novel Alanine-Zipper Trimer at 1.7 A Resolution, V13A,L16A,V20A,L23A,V27A,M30A,V34A mutations'''
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[[Category: Liu, J.]]
[[Category: Liu, J.]]
[[Category: Lu, M.]]
[[Category: Lu, M.]]
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[[Category: alanine-zipper]]
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[[Category: Alanine-zipper]]
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[[Category: coiled coil]]
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[[Category: Coiled coil]]
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[[Category: helix capping]]
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[[Category: Helix capping]]
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[[Category: lipoprotein]]
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[[Category: Lipoprotein]]
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[[Category: protein folding]]
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[[Category: Protein folding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:02:55 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:31:41 2008''
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Revision as of 18:02, 2 May 2008

Template:STRUCTURE 1jcc

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 Page seeded by OCA on Fri May 2 21:02:55 2008

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