1us8: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-{{Seed}}
-[[Image:1us8.png|left|200px]]
-<!--
+==The Rad50 signature motif: essential to ATP binding and biological function==
-The line below this paragraph, containing "STRUCTURE_1us8", creates the "Structure Box" on the page.
+<StructureSection load='1us8' size='340' side='right'caption='[[1us8]], [[Resolution|resolution]] 2.10&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'>[[1us8]] 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=1US8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1US8 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]] 2.1&#8491;</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=1us8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1us8 OCA], [https://pdbe.org/1us8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1us8 RCSB], [https://www.ebi.ac.uk/pdbsum/1us8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1us8 ProSAT]</span></td></tr>
-{{STRUCTURE_1us8|  PDB=1us8  |  SCENE=  }}
+</table>
+== Function ==
+[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/us/1us8_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=1us8 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The repair of double-strand breaks in DNA is an essential process in all organisms, and requires the coordinated activities of evolutionarily conserved protein assemblies. One of the most critical of these is the Mre11/Rad50 (M/R) complex, which is present in all three biological kingdoms, but is not well-understood at the biochemical level. Previous structural analysis of a Rad50 homolog from archaebacteria illuminated the catalytic core of the enzyme, an ATP-binding domain related to the ABC transporter family of ATPases. Here, we present the crystallographic structure of the Rad50 mutant S793R. This missense signature motif mutation changes the key serine residue in the signature motif that is conserved among Rad50 homologs and ABC ATPases. The S793R mutation is analogous to the mutation S549R in the cystic fibrosis transmembrane conductance regulator (CFTR) that results in cystic fibrosis. We show here that the serine to arginine change in the Rad50 protein prevents ATP binding and disrupts the communication among the other ATP-binding loops. This structural change, in turn, alters the communication between Rad50 monomers and thus prevents Rad50 dimerization. The equivalent mutation was made in the human Rad50 gene, and the resulting mutant protein did form a complex with Mre11 and Nbs1, but was specifically deficient in all ATP-dependent enzymatic activities. This signature motif structure-function homology extends to yeast, because the same mutation introduced into the Saccharomyces cerevisiae RAD50 gene generated an allele that failed to complement a rad50 deletion strain in DNA repair assays in vivo. These structural and biochemical results extend our understanding of the Rad50 catalytic domain and validate the use of the signature motif mutant to test the role of Rad50 ATP binding in diverse organisms.
-===THE RAD50 SIGNATURE MOTIF: ESSENTIAL TO ATP BINDING AND BIOLOGICAL FUNCTION===
+The rad50 signature motif: essential to ATP binding and biological function.,Moncalian G, Lengsfeld B, Bhaskara V, Hopfner KP, Karcher A, Alden E, Tainer JA, Paull TT J Mol Biol. 2004 Jan 23;335(4):937-51. PMID:14698290<ref>PMID:14698290</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_14698290}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1us8" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 14698290 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_14698290}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-US8 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1US8 OCA].
-==Reference==
-The rad50 signature motif: essential to ATP binding and biological function., Moncalian G, Lengsfeld B, Bhaskara V, Hopfner KP, Karcher A, Alden E, Tainer JA, Paull TT, J Mol Biol. 2004 Jan 23;335(4):937-51. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14698290 14698290]
-[[Category: Protein complex]]
 [[Category: Pyrococcus furiosus]]
-[[Category: Alden, E.]]
+[[Category: Alden E]]
-[[Category: Bhaskara, V.]]
+[[Category: Bhaskara V]]
-[[Category: Hopfner, K P.]]
+[[Category: Hopfner KP]]
-[[Category: Karcher, A.]]
+[[Category: Karcher A]]
-[[Category: Lengsfeld, B.]]
+[[Category: Lengsfeld B]]
-[[Category: Moncalian, G.]]
+[[Category: Moncalian G]]
-[[Category: Paull, T T.]]
+[[Category: Paull TT]]
-[[Category: Tainer, J A.]]
+[[Category: Tainer JA]]
-[[Category: Abc atpase]]
-[[Category: Dna repair]]
-[[Category: Signature motif]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 10:51:18 2008''