1wtq: Difference between revisions

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New page: left|200px<br /><applet load="1wtq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wtq, resolution 1.70Å" /> '''Hyperthermophile chr...
 
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[[Image:1wtq.gif|left|200px]]<br /><applet load="1wtq" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1wtq.gif|left|200px]]<br /><applet load="1wtq" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1wtq, resolution 1.70&Aring;" />
caption="1wtq, resolution 1.70&Aring;" />
'''Hyperthermophile chromosomal protein SAC7D single mutant M29F in complex with DNA GTAATTAC'''<br />
'''Hyperthermophile chromosomal protein SAC7D single mutant M29F in complex with DNA GTAATTAC'''<br />


==Overview==
==Overview==
Sac7d, a small, abundant, sequence-general DNA-binding protein from the, hyperthermophilic archaeon Sulfolobus acidocaldarius, causes a single-step, sharp kink in DNA (approximately 60 degrees) via the intercalation of both, Val26 and Met29. These two amino acids were systematically changed in size, to probe their effects on DNA kinking. Eight crystal structures of five, Sac7d mutant-DNA complexes have been analyzed. The DNA-binding pattern of, the V26A and M29A single mutants is similar to that of the wild-type, whereas the V26A/M29A protein binds DNA without side chain intercalation, resulting in a smaller overall bending (approximately 50 degrees). The, M29F mutant inserts the Phe29 side chain orthogonally to the C2pG3 step, without stacking with base pairs, inducing a sharp kink (approximately 80, degrees). In the V26F/M29F-GCGATCGC complex, Phe26 intercalates deeply, into DNA bases by stacking with the G3 base, whereas Phe29 is stacked on, the G15 deoxyribose, in a way similar to those used by the TATA, box-binding proteins. All mutants have reduced DNA-stabilizing ability, as, indicated by their lower T m values. The DNA kink patterns caused by, different combinations of hydrophobic side chains may be relevant in, understanding the manner by which other minor groove-binding proteins, interact with DNA.
Sac7d, a small, abundant, sequence-general DNA-binding protein from the hyperthermophilic archaeon Sulfolobus acidocaldarius, causes a single-step sharp kink in DNA (approximately 60 degrees) via the intercalation of both Val26 and Met29. These two amino acids were systematically changed in size to probe their effects on DNA kinking. Eight crystal structures of five Sac7d mutant-DNA complexes have been analyzed. The DNA-binding pattern of the V26A and M29A single mutants is similar to that of the wild-type, whereas the V26A/M29A protein binds DNA without side chain intercalation, resulting in a smaller overall bending (approximately 50 degrees). The M29F mutant inserts the Phe29 side chain orthogonally to the C2pG3 step without stacking with base pairs, inducing a sharp kink (approximately 80 degrees). In the V26F/M29F-GCGATCGC complex, Phe26 intercalates deeply into DNA bases by stacking with the G3 base, whereas Phe29 is stacked on the G15 deoxyribose, in a way similar to those used by the TATA box-binding proteins. All mutants have reduced DNA-stabilizing ability, as indicated by their lower T m values. The DNA kink patterns caused by different combinations of hydrophobic side chains may be relevant in understanding the manner by which other minor groove-binding proteins interact with DNA.


==About this Structure==
==About this Structure==
1WTQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_acidocaldarius Sulfolobus acidocaldarius]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WTQ OCA].  
1WTQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_acidocaldarius Sulfolobus acidocaldarius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WTQ OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Sulfolobus acidocaldarius]]
[[Category: Sulfolobus acidocaldarius]]
[[Category: Chen, C.J.]]
[[Category: Chen, C J.]]
[[Category: Chen, C.Y.]]
[[Category: Chen, C Y.]]
[[Category: Chou, C.C.]]
[[Category: Chou, C C.]]
[[Category: Ko, T.P.]]
[[Category: Ko, T P.]]
[[Category: Lin, T.W.]]
[[Category: Lin, T W.]]
[[Category: Wang, A.H.J.]]
[[Category: Wang, A H.J.]]
[[Category: archea]]
[[Category: archea]]
[[Category: complex chromatin protein/dna]]
[[Category: complex chromatin protein/dna]]
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[[Category: sac7d mutant]]
[[Category: sac7d mutant]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:40:05 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:47:59 2008''

Revision as of 16:48, 21 February 2008

File:1wtq.gif


1wtq, resolution 1.70Å

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Hyperthermophile chromosomal protein SAC7D single mutant M29F in complex with DNA GTAATTAC

OverviewOverview

Sac7d, a small, abundant, sequence-general DNA-binding protein from the hyperthermophilic archaeon Sulfolobus acidocaldarius, causes a single-step sharp kink in DNA (approximately 60 degrees) via the intercalation of both Val26 and Met29. These two amino acids were systematically changed in size to probe their effects on DNA kinking. Eight crystal structures of five Sac7d mutant-DNA complexes have been analyzed. The DNA-binding pattern of the V26A and M29A single mutants is similar to that of the wild-type, whereas the V26A/M29A protein binds DNA without side chain intercalation, resulting in a smaller overall bending (approximately 50 degrees). The M29F mutant inserts the Phe29 side chain orthogonally to the C2pG3 step without stacking with base pairs, inducing a sharp kink (approximately 80 degrees). In the V26F/M29F-GCGATCGC complex, Phe26 intercalates deeply into DNA bases by stacking with the G3 base, whereas Phe29 is stacked on the G15 deoxyribose, in a way similar to those used by the TATA box-binding proteins. All mutants have reduced DNA-stabilizing ability, as indicated by their lower T m values. The DNA kink patterns caused by different combinations of hydrophobic side chains may be relevant in understanding the manner by which other minor groove-binding proteins interact with DNA.

About this StructureAbout this Structure

1WTQ is a Single protein structure of sequence from Sulfolobus acidocaldarius. Full crystallographic information is available from OCA.

ReferenceReference

Probing the DNA kink structure induced by the hyperthermophilic chromosomal protein Sac7d., Chen CY, Ko TP, Lin TW, Chou CC, Chen CJ, Wang AH, Nucleic Acids Res. 2005 Jan 14;33(1):430-8. Print 2005. PMID:15653643

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