1wo3: Difference between revisions
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|PDB= 1wo3 |SIZE=350|CAPTION= <scene name='initialview01'>1wo3</scene> | |PDB= 1wo3 |SIZE=350|CAPTION= <scene name='initialview01'>1wo3</scene> | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Histone_acetyltransferase Histone acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.48 2.3.1.48] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone_acetyltransferase Histone acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.48 2.3.1.48] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1liq|1LIQ]], [[1wo4|1WO4]], [[1wo5|1WO5]], [[1wo6|1WO6]], [[1wo7|1WO7]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wo3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wo3 OCA], [http://www.ebi.ac.uk/pdbsum/1wo3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1wo3 RCSB]</span> | |||
}} | }} | ||
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==Overview== | ==Overview== | ||
Zinc binding motifs have received much attention in the area of protein design. Here, we have tested the suitability of a recently discovered nonnative zinc binding structure as a protein design scaffold. A series of multiple alanine mutants was created to investigate the minimal requirements for folding, and solution structures of these mutants showed that the original fold was maintained, despite changes in approximately 50% of the sequence. We next attempted to transplant binding faces from chosen bimolecular interactions onto one of these mutants, and many of the resulting "chimeras" were shown to adopt a native-like fold. These results both highlight the robust nature of small zinc binding domains and underscore the complexity of designing functional proteins, even using such small, highly ordered scaffolds as templates. | Zinc binding motifs have received much attention in the area of protein design. Here, we have tested the suitability of a recently discovered nonnative zinc binding structure as a protein design scaffold. A series of multiple alanine mutants was created to investigate the minimal requirements for folding, and solution structures of these mutants showed that the original fold was maintained, despite changes in approximately 50% of the sequence. We next attempted to transplant binding faces from chosen bimolecular interactions onto one of these mutants, and many of the resulting "chimeras" were shown to adopt a native-like fold. These results both highlight the robust nature of small zinc binding domains and underscore the complexity of designing functional proteins, even using such small, highly ordered scaffolds as templates. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Sharpe, B K.]] | [[Category: Sharpe, B K.]] | ||
[[Category: Wilce, J A.]] | [[Category: Wilce, J A.]] | ||
[[Category: protein design]] | [[Category: protein design]] | ||
[[Category: zinc finger]] | [[Category: zinc finger]] | ||
''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 00:38:51 2008'' | ||
Revision as of 00:38, 31 March 2008
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| Ligands: | |||||||
| Activity: | Histone acetyltransferase, with EC number 2.3.1.48 | ||||||
| Related: | 1LIQ, 1WO4, 1WO5, 1WO6, 1WO7
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Solution structure of Minimal Mutant 1 (MM1): Multiple alanine mutant of non-native CHANCE domain
OverviewOverview
Zinc binding motifs have received much attention in the area of protein design. Here, we have tested the suitability of a recently discovered nonnative zinc binding structure as a protein design scaffold. A series of multiple alanine mutants was created to investigate the minimal requirements for folding, and solution structures of these mutants showed that the original fold was maintained, despite changes in approximately 50% of the sequence. We next attempted to transplant binding faces from chosen bimolecular interactions onto one of these mutants, and many of the resulting "chimeras" were shown to adopt a native-like fold. These results both highlight the robust nature of small zinc binding domains and underscore the complexity of designing functional proteins, even using such small, highly ordered scaffolds as templates.
About this StructureAbout this Structure
1WO3 is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
ReferenceReference
Assessment of the robustness of a serendipitous zinc binding fold: mutagenesis and protein grafting., Sharpe BK, Liew CK, Kwan AH, Wilce JA, Crossley M, Matthews JM, Mackay JP, Structure. 2005 Feb;13(2):257-66. PMID:15698569
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