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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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== | ==Hyperthermophile chromosomal protein SAC7D single mutant M29F in complex with DNA GTAATTAC== | ||
Sac7d, a small, abundant, sequence-general DNA-binding protein from the | <StructureSection load='1wtq' size='340' side='right'caption='[[1wtq]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1wtq]] is a 3 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WTQ FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1wtq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wtq OCA], [https://pdbe.org/1wtq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wtq RCSB], [https://www.ebi.ac.uk/pdbsum/1wtq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wtq ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/DN7D_SULAC DN7D_SULAC] Can constrain negative DNA supercoils. May be involved in maintaining the integrity of the genome at high temperature.[UniProtKB:P61990] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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<ref>PMID:15653643</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: | <div class="pdbe-citations 1wtq" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Sulfolobus acidocaldarius]] | [[Category: Sulfolobus acidocaldarius]] | ||
[[Category: Chen | [[Category: Chen C-J]] | ||
[[Category: Chen | [[Category: Chen C-Y]] | ||
[[Category: Chou | [[Category: Chou C-C]] | ||
[[Category: Ko | [[Category: Ko T-P]] | ||
[[Category: Lin | [[Category: Lin T-W]] | ||
[[Category: Wang | [[Category: Wang AH-J]] | ||
Latest revision as of 13:29, 16 August 2023
Hyperthermophile chromosomal protein SAC7D single mutant M29F in complex with DNA GTAATTACHyperthermophile chromosomal protein SAC7D single mutant M29F in complex with DNA GTAATTAC
Structural highlights
FunctionDN7D_SULAC Can constrain negative DNA supercoils. May be involved in maintaining the integrity of the genome at high temperature.[UniProtKB:P61990] Publication Abstract from PubMedSac7d, 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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