1le8: Difference between revisions
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|PDB= 1le8 |SIZE=350|CAPTION= <scene name='initialview01'>1le8</scene>, resolution 2.30Å | |PDB= 1le8 |SIZE=350|CAPTION= <scene name='initialview01'>1le8</scene>, resolution 2.30Å | ||
|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= <scene name='pdbligand=DA:2'-DEOXYADENOSINE-5'-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5'-MONOPHOSPHATE'>DT</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= MATalpha2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | |GENE= MATalpha2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1yrn|1YRN]], [[1akh|1AKH]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1le8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1le8 OCA], [http://www.ebi.ac.uk/pdbsum/1le8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1le8 RCSB]</span> | |||
}} | }} | ||
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[[Category: protein-dna complex]] | [[Category: protein-dna complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:01:50 2008'' | ||
Revision as of 22:01, 30 March 2008
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| , resolution 2.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Gene: | MATalpha2 (Saccharomyces cerevisiae) | ||||||
| Related: | 1YRN, 1AKH
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of the MATa1/MATalpha2-3A Heterodimer Bound to DNA Complex
OverviewOverview
Triply mutated MATalpha2 protein, alpha2-3A, in which all three major groove-contacting residues are mutated to alanine, is defective in binding DNA alone or in complex with Mcm1 yet binds with MATa1 with near wild-type affinity and specificity. To gain insight into this unexpected behavior, we determined the crystal structure of the a1/alpha2-3A/DNA complex. The structure shows that the triple mutation causes a collapse of the alpha2-3A/DNA interface that results in a reorganized set of alpha2-3A/DNA contacts, thereby enabling the mutant protein to recognize the wild-type DNA sequence. Isothermal titration calorimetry measurements reveal that a much more favorable entropic component stabilizes the a1/alpha2-3A/DNA complex than the alpha2-3A/DNA complex. The combined structural and thermodynamic studies provide an explanation of how partner proteins influence the sequence specificity of a DNA binding protein.
About this StructureAbout this Structure
1LE8 is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
Structural and thermodynamic characterization of the DNA binding properties of a triple alanine mutant of MATalpha2., Ke A, Mathias JR, Vershon AK, Wolberger C, Structure. 2002 Jul;10(7):961-71. PMID:12121651
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