1bb1
From Proteopedia
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| - | [[Image:1bb1.gif|left|200px]] | + | [[Image:1bb1.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF A DESIGNED, THERMOSTABLE HETEROTRIMERIC COILED COIL''' | + | {{Structure |
| + | |PDB= 1bb1 |SIZE=350|CAPTION= <scene name='initialview01'>1bb1</scene>, resolution 1.8Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene> and <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF A DESIGNED, THERMOSTABLE HETEROTRIMERIC COILED COIL''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1BB1 is a [ | + | 1BB1 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BB1 OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of a designed, thermostable, heterotrimeric coiled coil., Nautiyal S, Alber T, Protein Sci. 1999 Jan;8(1):84-90. PMID:[http:// | + | Crystal structure of a designed, thermostable, heterotrimeric coiled coil., Nautiyal S, Alber T, Protein Sci. 1999 Jan;8(1):84-90. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10210186 10210186] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Synthetic construct]] | [[Category: Synthetic construct]] | ||
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[[Category: de novo protein design]] | [[Category: de novo protein design]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:08:39 2008'' |
Revision as of 08:08, 20 March 2008
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| , resolution 1.8Å | |||||||
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| Ligands: | , and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF A DESIGNED, THERMOSTABLE HETEROTRIMERIC COILED COIL
Overview
Electrostatic interactions are often critical for determining the specificity of protein-protein complexes. To study the role of electrostatic interactions for assembly of helical bundles, we previously designed a thermostable, heterotrimeric coiled coil, ABC, in which charged residues were employed to drive preferential association of three distinct, 34-residue helices. To investigate the basis for heterotrimer specificity, we have used multiwavelength anomalous diffraction (MAD) analysis to determine the 1.8 A resolution crystal structure of ABC. The structure shows that ABC forms a heterotrimeric coiled coil with the intended arrangement of parallel chains. Over half of the ion pairs engineered to restrict helix associations were apparent in the experimental electron density map. As seen in other trimeric coiled coils, ABC displays acute knobs-into-holes packing and a buried anion coordinated by core polar amino acids. These interactions validate the design strategy and illustrate how packing and polar contacts determine structural uniqueness.
About this Structure
1BB1 is a Protein complex structure of sequences from Synthetic construct. Full crystallographic information is available from OCA.
Reference
Crystal structure of a designed, thermostable, heterotrimeric coiled coil., Nautiyal S, Alber T, Protein Sci. 1999 Jan;8(1):84-90. PMID:10210186
Page seeded by OCA on Thu Mar 20 10:08:39 2008
