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- PDB-4fis: THE MOLECULAR STRUCTURE OF WILD-TYPE AND A MUTANT FIS PROTEIN: RE... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4fis | ||||||
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Title | THE MOLECULAR STRUCTURE OF WILD-TYPE AND A MUTANT FIS PROTEIN: RELATIONSHIP BETWEEN MUTATIONAL CHANGES AND RECOMBINATIONAL ENHANCER FUNCTION OR DNA BINDING | ||||||
![]() | FACTOR FOR INVERSION STIMULATION (FIS) | ||||||
![]() | DNA BINDING PROTEIN / DNA-BINDING PROTEIN | ||||||
Function / homology | ![]() invertasome / positive regulation of DNA recombination / sequence-specific DNA binding, bending / provirus excision / nucleoid / DNA-binding transcription repressor activity / DNA-binding transcription activator activity / chromosome organization / core promoter sequence-specific DNA binding / protein-DNA complex ...invertasome / positive regulation of DNA recombination / sequence-specific DNA binding, bending / provirus excision / nucleoid / DNA-binding transcription repressor activity / DNA-binding transcription activator activity / chromosome organization / core promoter sequence-specific DNA binding / protein-DNA complex / response to radiation / nucleosome / sequence-specific DNA binding / transcription cis-regulatory region binding / DNA-templated transcription / regulation of DNA-templated transcription / protein homodimerization activity / DNA binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Yuan, H.S. / Finkel, S.E. / Feng, J.-A. / Johnson, R.C. / Dickerson, R.E. | ||||||
![]() | ![]() Title: The molecular structure of wild-type and a mutant Fis protein: relationship between mutational changes and recombinational enhancer function or DNA binding. Authors: Yuan, H.S. / Finkel, S.E. / Feng, J.A. / Kaczor-Grzeskowiak, M. / Johnson, R.C. / Dickerson, R.E. | ||||||
History |
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Remark 650 | HELIX THE EXTENDED REGIONS BEFORE A-HELIX (RESIDUES A 20 TO A 25 AND B 20 TO B 25) AND AFTER A- ...HELIX THE EXTENDED REGIONS BEFORE A-HELIX (RESIDUES A 20 TO A 25 AND B 20 TO B 25) AND AFTER A-HELIX (RESIDUES A 43 TO A 46 AND B 43 TO B 46) ARE MORE FLEXIBLE. THE STRUCTURE IN THESE REGIONS IS ILL-DEFINED AND THE ATOMS HAVE HIGH TEMPERATURE FACTORS. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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PDBx/mmCIF format | ![]() | 39.7 KB | Display | ![]() |
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PDB format | ![]() | 28.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 11198.867 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.1 Å3/Da / Density % sol: 41.57 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 8.2 / Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 2.3 Å / Num. all: 16603 / Num. obs: 6184 / Rmerge F obs: 0.0392 |
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Processing
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Refinement | Rfactor Rwork: 0.185 / Rfactor obs: 0.185 / Highest resolution: 2.3 Å | ||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.3 Å
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Refinement | *PLUS Highest resolution: 2.3 Å / Num. reflection obs: 5913 / σ(F): 2 / Rfactor obs: 0.185 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS | ||||||||||||
Refine LS restraints | *PLUS
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