2rhf

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (01:24, 21 November 2024) (edit) (undo)
 
(8 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:2rhf.png|left|200px]]
 
-
<!--
+
==D. radiodurans RecQ HRDC domain 3==
-
The line below this paragraph, containing "STRUCTURE_2rhf", creates the "Structure Box" on the page.
+
<StructureSection load='2rhf' size='340' side='right'caption='[[2rhf]], [[Resolution|resolution]] 1.10&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[2rhf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Deinococcus_radiodurans_R1 Deinococcus radiodurans R1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RHF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RHF FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.1&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-
{{STRUCTURE_2rhf| PDB=2rhf | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2rhf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rhf OCA], [https://pdbe.org/2rhf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rhf RCSB], [https://www.ebi.ac.uk/pdbsum/2rhf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rhf ProSAT]</span></td></tr>
 +
</table>
 +
== 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/rh/2rhf_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2rhf ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
RecQ helicases are critical for maintaining genome integrity in organisms ranging from bacteria to humans by participating in a complex network of DNA metabolic pathways. Their diverse cellular functions require specialization and coordination of multiple protein domains that integrate catalytic functions with DNA-protein and protein-protein interactions. The RecQ helicase from Deinococcus radiodurans (DrRecQ) is unusual among RecQ family members in that it has evolved to utilize three 'Helicase and RNaseD C-terminal' (HRDC) domains to regulate its activity. In this report, we describe the high-resolution structure of the C-terminal-most HRDC domain of DrRecQ. The structure reveals unusual electrostatic surface features that distinguish it from other HRDC domains. Mutation of individual residues in these regions affects the DNA binding affinity of DrRecQ and its ability to unwind a partial duplex DNA substrate. Taken together, the results suggest the unusual electrostatic surface features of the DrRecQ HRDC domain may be important for inter-domain interactions that regulate structure-specific DNA binding and help direct DrRecQ to specific recombination/repair sites.
-
===D. radiodurans RecQ HRDC domain 3===
+
Structure and function of the regulatory C-terminal HRDC domain from Deinococcus radiodurans RecQ.,Killoran MP, Keck JL Nucleic Acids Res. 2008 May;36(9):3139-49. Epub 2008 Apr 13. PMID:18411208<ref>PMID:18411208</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 2rhf" style="background-color:#fffaf0;"></div>
-
<!--
+
==See Also==
-
The line below this paragraph, {{ABSTRACT_PUBMED_18411208}}, adds the Publication Abstract to the page
+
*[[Helicase 3D structures|Helicase 3D structures]]
-
(as it appears on PubMed at http://www.pubmed.gov), where 18411208 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_18411208}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
[[Category: Deinococcus radiodurans R1]]
-
2RHF is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans_r1 Deinococcus radiodurans r1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RHF OCA].
+
[[Category: Large Structures]]
-
 
+
[[Category: Keck JL]]
-
==Reference==
+
[[Category: Killoran MP]]
-
<ref group="xtra">PMID:18411208</ref><references group="xtra"/>
+
-
[[Category: Deinococcus radiodurans r1]]
+
-
[[Category: Keck, J L.]]
+
-
[[Category: Killoran, M P.]]
+
-
[[Category: Atp-binding]]
+
-
[[Category: D. radioduran]]
+
-
[[Category: Helicase]]
+
-
[[Category: Hrdc]]
+
-
[[Category: Hydrolase]]
+
-
[[Category: Nucleotide-binding]]
+
-
[[Category: Recq]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 17:47:08 2009''
+

Current revision

D. radiodurans RecQ HRDC domain 3

PDB ID 2rhf

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools