1zsz
From Proteopedia
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|PDB= 1zsz |SIZE=350|CAPTION= <scene name='initialview01'>1zsz</scene>, resolution 2.00Å | |PDB= 1zsz |SIZE=350|CAPTION= <scene name='initialview01'>1zsz</scene>, resolution 2.00Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene> | + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= sspB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=727 Haemophilus influenzae]) | |GENE= sspB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=727 Haemophilus influenzae]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zsz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zsz OCA], [http://www.ebi.ac.uk/pdbsum/1zsz PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zsz RCSB]</span> | ||
}} | }} | ||
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[[Category: Grant, R A.]] | [[Category: Grant, R A.]] | ||
[[Category: Sauer, R T.]] | [[Category: Sauer, R T.]] | ||
| - | [[Category: MG]] | ||
[[Category: aaa]] | [[Category: aaa]] | ||
[[Category: adaptor]] | [[Category: adaptor]] | ||
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[[Category: specificity]] | [[Category: specificity]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:41:18 2008'' |
Revision as of 22:41, 30 March 2008
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| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | sspB (Haemophilus influenzae) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of a computationally designed SspB heterodimer
Overview
Protein-protein interactions can be designed computationally by using positive strategies that maximize the stability of the desired structure and/or by negative strategies that seek to destabilize competing states. Here, we compare the efficacy of these methods in reengineering a protein homodimer into a heterodimer. The stability-design protein (positive design only) was experimentally more stable than the specificity-design heterodimer (positive and negative design). By contrast, only the specificity-design protein assembled as a homogenous heterodimer in solution, whereas the stability-design protein formed a mixture of homodimer and heterodimer species. The experimental stabilities of the engineered proteins correlated roughly with their calculated stabilities, and the crystal structure of the specificity-design heterodimer showed most of the predicted side-chain packing interactions and a main-chain conformation indistinguishable from the wild-type structure. These results indicate that the design simulations capture important features of both stability and structure and demonstrate that negative design can be critical for attaining specificity when competing states are close in structure space.
About this Structure
1ZSZ is a Protein complex structure of sequences from Haemophilus influenzae. Full crystallographic information is available from OCA.
Reference
Specificity versus stability in computational protein design., Bolon DN, Grant RA, Baker TA, Sauer RT, Proc Natl Acad Sci U S A. 2005 Sep 6;102(36):12724-9. Epub 2005 Aug 29. PMID:16129838
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