1jcd: Difference between revisions

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[[Image:1jcd.gif|left|200px]]<br /><applet load="1jcd" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1jcd.gif|left|200px]]<br /><applet load="1jcd" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1jcd, resolution 1.30Å" />

'''Crystal Structure of a Novel Alanine-Zipper Trimer at 1.3 A Resolution, I6A,L9A,V13A,L16A,V20A,L23A,V27A,M30A,V34A,L48A,M51A mutations'''<br />

==Overview==

A major challenge in protein folding is to identify and quantify specific, structural determinants that allow native proteins to acquire their unique, folded structures. Here we report the engineering of a 52-residue protein, (Ala-14) that contains exclusively alanine residues at the hydrophobic a, and d positions of a natural heptad-repeat sequence. Ala-14 is unfolded, under normal solution conditions yet forms a parallel three-stranded, alpha-helical coiled coil in crystals. Ala-14 trimers in the solid state, associate with each other through the pairing of polar side chains and, formation of an extended network of water-mediated hydrogen bonds. In, contrast to the classical view that local intramolecular tertiary, interactions dictate the three-dimensional structure of small, single-domain proteins, Ala-14 shows that long range intermolecular, interactions can be essential in determining the metastable alanine-zipper, structure. A similar interplay between short range local and longer range, global forces may underlie the conformational properties of the growing, class of natively unstructured proteins in biological processes.

A major challenge in protein folding is to identify and quantify specific structural determinants that allow native proteins to acquire their unique folded structures. Here we report the engineering of a 52-residue protein (Ala-14) that contains exclusively alanine residues at the hydrophobic a and d positions of a natural heptad-repeat sequence. Ala-14 is unfolded under normal solution conditions yet forms a parallel three-stranded alpha-helical coiled coil in crystals. Ala-14 trimers in the solid state associate with each other through the pairing of polar side chains and formation of an extended network of water-mediated hydrogen bonds. In contrast to the classical view that local intramolecular tertiary interactions dictate the three-dimensional structure of small single-domain proteins, Ala-14 shows that long range intermolecular interactions can be essential in determining the metastable alanine-zipper structure. A similar interplay between short range local and longer range global forces may underlie the conformational properties of the growing class of natively unstructured proteins in biological processes.

==About this Structure==

1JCD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1JCD OCA].

1JCD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JCD OCA].

==Reference==

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[[Category: protein folding]]

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@@ Line 1: / Line 1: @@
-[[Image:1jcd.gif|left|200px]]<br /><applet load="1jcd" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1jcd.gif|left|200px]]<br /><applet load="1jcd" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1jcd, resolution 1.30&Aring;" />
 '''Crystal Structure of a Novel Alanine-Zipper Trimer at 1.3 A Resolution, I6A,L9A,V13A,L16A,V20A,L23A,V27A,M30A,V34A,L48A,M51A mutations'''<br />
 ==Overview==
-A major challenge in protein folding is to identify and quantify specific, structural determinants that allow native proteins to acquire their unique, folded structures. Here we report the engineering of a 52-residue protein, (Ala-14) that contains exclusively alanine residues at the hydrophobic a, and d positions of a natural heptad-repeat sequence. Ala-14 is unfolded, under normal solution conditions yet forms a parallel three-stranded, alpha-helical coiled coil in crystals. Ala-14 trimers in the solid state, associate with each other through the pairing of polar side chains and, formation of an extended network of water-mediated hydrogen bonds. In, contrast to the classical view that local intramolecular tertiary, interactions dictate the three-dimensional structure of small, single-domain proteins, Ala-14 shows that long range intermolecular, interactions can be essential in determining the metastable alanine-zipper, structure. A similar interplay between short range local and longer range, global forces may underlie the conformational properties of the growing, class of natively unstructured proteins in biological processes.
+A major challenge in protein folding is to identify and quantify specific structural determinants that allow native proteins to acquire their unique folded structures. Here we report the engineering of a 52-residue protein (Ala-14) that contains exclusively alanine residues at the hydrophobic a and d positions of a natural heptad-repeat sequence. Ala-14 is unfolded under normal solution conditions yet forms a parallel three-stranded alpha-helical coiled coil in crystals. Ala-14 trimers in the solid state associate with each other through the pairing of polar side chains and formation of an extended network of water-mediated hydrogen bonds. In contrast to the classical view that local intramolecular tertiary interactions dictate the three-dimensional structure of small single-domain proteins, Ala-14 shows that long range intermolecular interactions can be essential in determining the metastable alanine-zipper structure. A similar interplay between short range local and longer range global forces may underlie the conformational properties of the growing class of natively unstructured proteins in biological processes.
 ==About this Structure==
-JCD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JCD OCA].
+JCD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JCD OCA].
 ==Reference==
@@ Line 21: / Line 21: @@
 [[Category: protein folding]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:06:22 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:21:06 2008''