3kde: Difference between revisions

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==Crystal structure of the THAP domain from D. melanogaster P-element transposase in complex with its natural DNA binding site==
==Crystal structure of the THAP domain from D. melanogaster P-element transposase in complex with its natural DNA binding site==
<StructureSection load='3kde' size='340' side='right' caption='[[3kde]], [[Resolution|resolution]] 1.74&Aring;' scene=''>
<StructureSection load='3kde' size='340' side='right' caption='[[3kde]], [[Resolution|resolution]] 1.74&Aring;' scene=''>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=BRU:5-BROMO-2-DEOXYURIDINE-5-MONOPHOSPHATE'>BRU</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=BRU:5-BROMO-2-DEOXYURIDINE-5-MONOPHOSPHATE'>BRU</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">T ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">T ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3kde FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kde OCA], [http://pdbe.org/3kde PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3kde RCSB], [http://www.ebi.ac.uk/pdbsum/3kde PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3kde FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kde OCA], [http://pdbe.org/3kde PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3kde RCSB], [http://www.ebi.ac.uk/pdbsum/3kde PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3kde ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kd/3kde_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kd/3kde_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>

Revision as of 12:18, 26 December 2018

Crystal structure of the THAP domain from D. melanogaster P-element transposase in complex with its natural DNA binding siteCrystal structure of the THAP domain from D. melanogaster P-element transposase in complex with its natural DNA binding site

Structural highlights

3kde is a 3 chain structure with sequence from Drome. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Gene:T (DROME)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PELET_DROME] P-element transposase that specifically mediates transposition of P-elements. Mediates both; precise and imprecise excision.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

THAP-family C(2)CH zinc-coordinating DNA-binding proteins function in diverse eukaryotic cellular processes, such as transposition, transcriptional repression, stem-cell pluripotency, angiogenesis and neurological function. To determine the molecular basis for sequence-specific DNA recognition by THAP proteins, we solved the crystal structure of the Drosophila melanogaster P element transposase THAP domain (DmTHAP) in complex with a natural 10-base-pair site. In contrast to C(2)H(2) zinc fingers, DmTHAP docks a conserved beta-sheet into the major groove and a basic C-terminal loop into the adjacent minor groove. We confirmed specific protein-DNA interactions by mutagenesis and DNA-binding assays. Sequence analysis of natural and in vitro-selected binding sites suggests that several THAPs (DmTHAP and human THAP1 and THAP9) recognize a bipartite TXXGGGX(A/T) consensus motif; homology suggests THAP proteins bind DNA through a bipartite interaction. These findings reveal the conserved mechanisms by which THAP-family proteins engage specific chromosomal target elements.

THAP proteins target specific DNA sites through bipartite recognition of adjacent major and minor grooves.,Sabogal A, Lyubimov AY, Corn JE, Berger JM, Rio DC Nat Struct Mol Biol. 2010 Jan;17(1):117-23. Epub 2009 Dec 13. PMID:20010837[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Rio DC, Laski FA, Rubin GM. Identification and immunochemical analysis of biologically active Drosophila P element transposase. Cell. 1986 Jan 17;44(1):21-32. PMID:2416475
  2. Sabogal A, Lyubimov AY, Corn JE, Berger JM, Rio DC. THAP proteins target specific DNA sites through bipartite recognition of adjacent major and minor grooves. Nat Struct Mol Biol. 2010 Jan;17(1):117-23. Epub 2009 Dec 13. PMID:20010837 doi:10.1038/nsmb.1742
  3. Sabogal A, Lyubimov AY, Corn JE, Berger JM, Rio DC. THAP proteins target specific DNA sites through bipartite recognition of adjacent major and minor grooves. Nat Struct Mol Biol. 2010 Jan;17(1):117-23. Epub 2009 Dec 13. PMID:20010837 doi:10.1038/nsmb.1742

3kde, resolution 1.74Å

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