1f2t: Difference between revisions
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New page: left|200px<br /><applet load="1f2t" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f2t, resolution 1.6Å" /> '''CRYSTAL STRUCTURE OF ... |
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== | ==Crystal Structure of ATP-Free RAD50 ABC-ATPase== | ||
<StructureSection load='1f2t' size='340' side='right'caption='[[1f2t]], [[Resolution|resolution]] 1.60Å' scene=''> | |||
== Structural highlights == | |||
== | <table><tr><td colspan='2'>[[1f2t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F2T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F2T 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]] 1.6Å</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=1f2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f2t OCA], [https://pdbe.org/1f2t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f2t RCSB], [https://www.ebi.ac.uk/pdbsum/1f2t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f2t ProSAT]</span></td></tr> | |||
== | </table> | ||
== Function == | |||
[[Category: | [https://www.uniprot.org/uniprot/RAD50_PYRFU RAD50_PYRFU] Involved in DNA double-strand break repair (DSBR). The Rad50/Mre11 complex possesses single-strand endonuclease activity and ATP-dependent double-strand-specific 3'-5' exonuclease activity. Rad50 provides an ATP-dependent control of Mre11 by unwinding and/or repositioning DNA ends into the Mre11 active site.[HAMAP-Rule:MF_00449] | ||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f2/1f2t_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1f2t ConSurf]. | |||
<div style="clear:both"></div> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pyrococcus furiosus]] | [[Category: Pyrococcus furiosus]] | ||
[[Category: Craig | [[Category: Craig L]] | ||
[[Category: Hopfner | [[Category: Hopfner KP]] | ||
[[Category: Karcher | [[Category: Karcher A]] | ||
[[Category: Shin | [[Category: Shin DS]] | ||
Latest revision as of 10:09, 7 February 2024
Crystal Structure of ATP-Free RAD50 ABC-ATPaseCrystal Structure of ATP-Free RAD50 ABC-ATPase
Structural highlights
FunctionRAD50_PYRFU Involved in DNA double-strand break repair (DSBR). The Rad50/Mre11 complex possesses single-strand endonuclease activity and ATP-dependent double-strand-specific 3'-5' exonuclease activity. Rad50 provides an ATP-dependent control of Mre11 by unwinding and/or repositioning DNA ends into the Mre11 active site.[HAMAP-Rule:MF_00449] Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. |
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