1tgg
From Proteopedia
(New page: 200px<br /><applet load="1tgg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tgg, resolution 2.0Å" /> '''RH3 DESIGNED RIGHT-HA...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1tgg.gif|left|200px]]<br /><applet load="1tgg" size=" | + | [[Image:1tgg.gif|left|200px]]<br /><applet load="1tgg" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1tgg, resolution 2.0Å" /> | caption="1tgg, resolution 2.0Å" /> | ||
'''RH3 DESIGNED RIGHT-HANDED COILED COIL TRIMER'''<br /> | '''RH3 DESIGNED RIGHT-HANDED COILED COIL TRIMER'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Designing new protein folds requires a method for simultaneously | + | Designing new protein folds requires a method for simultaneously optimizing the conformation of the backbone and the side-chains. One approach to this problem is the use of a parameterized backbone, which allows the systematic exploration of families of structures. We report the crystal structure of RH3, a right-handed, three-helix coiled coil that was designed using a parameterized backbone and detailed modeling of core packing. This crystal structure was determined using another rationally designed feature, a metal-binding site that permitted experimental phasing of the X-ray data. RH3 adopted the intended fold, which has not been observed previously in biological proteins. Unanticipated structural asymmetry in the trimer was a principal source of variation within the RH3 structure. The sequence of RH3 differs from that of a previously characterized right-handed tetramer, RH4, at only one position in each 11 amino acid sequence repeat. This close similarity indicates that the design method is sensitive to the core packing interactions that specify the protein structure. Comparison of the structures of RH3 and RH4 indicates that both steric overlap and cavity formation provide strong driving forces for oligomer specificity. |
==About this Structure== | ==About this Structure== | ||
| - | 1TGG is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with NI, CL and ACE as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1TGG is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=NI:'>NI</scene>, <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=ACE:'>ACE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TGG OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Alber, T.]] | [[Category: Alber, T.]] | ||
| - | [[Category: Harbury, P | + | [[Category: Harbury, P B.]] |
| - | [[Category: Kim, P | + | [[Category: Kim, P S.]] |
| - | [[Category: Plecs, J | + | [[Category: Plecs, J J.]] |
[[Category: ACE]] | [[Category: ACE]] | ||
[[Category: CL]] | [[Category: CL]] | ||
| Line 21: | Line 21: | ||
[[Category: coiled coil; de novo design]] | [[Category: coiled coil; de novo design]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:13:16 2008'' |
Revision as of 13:13, 21 February 2008
|
RH3 DESIGNED RIGHT-HANDED COILED COIL TRIMER
Overview
Designing new protein folds requires a method for simultaneously optimizing the conformation of the backbone and the side-chains. One approach to this problem is the use of a parameterized backbone, which allows the systematic exploration of families of structures. We report the crystal structure of RH3, a right-handed, three-helix coiled coil that was designed using a parameterized backbone and detailed modeling of core packing. This crystal structure was determined using another rationally designed feature, a metal-binding site that permitted experimental phasing of the X-ray data. RH3 adopted the intended fold, which has not been observed previously in biological proteins. Unanticipated structural asymmetry in the trimer was a principal source of variation within the RH3 structure. The sequence of RH3 differs from that of a previously characterized right-handed tetramer, RH4, at only one position in each 11 amino acid sequence repeat. This close similarity indicates that the design method is sensitive to the core packing interactions that specify the protein structure. Comparison of the structures of RH3 and RH4 indicates that both steric overlap and cavity formation provide strong driving forces for oligomer specificity.
About this Structure
1TGG is a Protein complex structure of sequences from [1] with , and as ligands. Full crystallographic information is available from OCA.
Reference
Structural test of the parameterized-backbone method for protein design., Plecs JJ, Harbury PB, Kim PS, Alber T, J Mol Biol. 2004 Sep 3;342(1):289-97. PMID:15313624
Page seeded by OCA on Thu Feb 21 15:13:16 2008
Categories: Protein complex | Alber, T. | Harbury, P B. | Kim, P S. | Plecs, J J. | ACE | CL | NI | Coiled coil; de novo design
