1qu5

From Proteopedia

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Current revision

NMR STRUCTURE OF A NEW PHOSPHOTYROSINE BINDING DOMAIN CONTAINING THE FHA2 DOMAIN OF RAD 53

Structural highlights

1qu5 is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RAD53_YEAST Controls S-phase checkpoint as well as G1 and G2 DNA damage checkpoints. Phosphorylates proteins on serine, threonine, and tyrosine. Prevents entry into anaphase and mitotic exit after DNA damage via regulation of the Polo kinase CDC5. Seems to be involved in the phosphorylation of RPH1.^[1] ^[2] ^[3] ^[4] ^[5]

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

The forkhead-associated (FHA) domain is a 55-75 amino acid residue module found in >20 proteins from yeast to human. It has been suggested to participate in signal transduction pathways, perhaps via protein-protein interactions involving recognition of phosphopeptides. Neither the structure nor the ligand of FHA is known. Yeast Rad53, a checkpoint protein involved in DNA damage response, contains two FHA domains, FHA1 (residues 66-116) and FHA2 (residues 601-664), the second of which recognizes phosphorylated Rad9. We herein report the solution structure of an "FHA2-containing domain" of Rad53 (residues 573-730). The structure consists of a beta-sandwich containing two antiparallel beta-sheets and a short, C-terminal alpha-helix. Binding experiments suggested that the FHA2-containing domain specifically recognizes pTyr and a pTyr-containing peptide from Rad9, and that the binding site involves residues highly conserved across FHA domains. The results, along with other recent reports, suggest that FHA domains could have pTyr and pSer/Thr dual specificity.

Structure and function of a new phosphopeptide-binding domain containing the FHA2 of Rad53.,Liao H, Byeon IJ, Tsai MD J Mol Biol. 1999 Dec 10;294(4):1041-9. PMID:10588905^[6]

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

References

↑ Zheng P, Fay DS, Burton J, Xiao H, Pinkham JL, Stern DF. SPK1 is an essential S-phase-specific gene of Saccharomyces cerevisiae that encodes a nuclear serine/threonine/tyrosine kinase. Mol Cell Biol. 1993 Sep;13(9):5829-42. PMID:8355715
↑ Allen JB, Zhou Z, Siede W, Friedberg EC, Elledge SJ. The SAD1/RAD53 protein kinase controls multiple checkpoints and DNA damage-induced transcription in yeast. Genes Dev. 1994 Oct 15;8(20):2401-15. PMID:7958905
↑ Sanchez Y, Bachant J, Wang H, Hu F, Liu D, Tetzlaff M, Elledge SJ. Control of the DNA damage checkpoint by chk1 and rad53 protein kinases through distinct mechanisms. Science. 1999 Nov 5;286(5442):1166-71. PMID:10550056
↑ Kim EM, Jang YK, Park SD. Phosphorylation of Rph1, a damage-responsive repressor of PHR1 in Saccharomyces cerevisiae, is dependent upon Rad53 kinase. Nucleic Acids Res. 2002 Feb 1;30(3):643-8. PMID:11809875
↑ Pike BL, Yongkiettrakul S, Tsai MD, Heierhorst J. Mdt1, a novel Rad53 FHA1 domain-interacting protein, modulates DNA damage tolerance and G(2)/M cell cycle progression in Saccharomyces cerevisiae. Mol Cell Biol. 2004 Apr;24(7):2779-88. PMID:15024067
↑ Liao H, Byeon IJ, Tsai MD. Structure and function of a new phosphopeptide-binding domain containing the FHA2 of Rad53. J Mol Biol. 1999 Dec 10;294(4):1041-9. PMID:10588905 doi:10.1006/jmbi.1999.3313

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1qu5"

Categories: Large Structures | Saccharomyces cerevisiae | Byeon I-JL | Liao H | Tsai M-D

@@ Line 1: / Line 1: @@
-[[Image:1qu5.jpg|left|200px]]<br /><applet load="1qu5" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1qu5" />
-'''NMR STRUCTURE OF A NEW PHOSPHOTYROSINE BINDING DOMAIN CONTAINING THE FHA2 DOMAIN OF RAD 53'''<br />
-==Overview==
+==NMR STRUCTURE OF A NEW PHOSPHOTYROSINE BINDING DOMAIN CONTAINING THE FHA2 DOMAIN OF RAD 53==
-The forkhead-associated (FHA) domain is a 55-75 amino acid residue module, found in &gt;20 proteins from yeast to human. It has been suggested to, participate in signal transduction pathways, perhaps via protein-protein, interactions involving recognition of phosphopeptides. Neither the, structure nor the ligand of FHA is known. Yeast Rad53, a checkpoint, protein involved in DNA damage response, contains two FHA domains, FHA1, (residues 66-116) and FHA2 (residues 601-664), the second of which, recognizes phosphorylated Rad9. We herein report the solution structure of, an "FHA2-containing domain" of Rad53 (residues 573-730). The structure, consists of a beta-sandwich containing two antiparallel beta-sheets and a, short, C-terminal alpha-helix. Binding experiments suggested that the, FHA2-containing domain specifically recognizes pTyr and a pTyr-containing, peptide from Rad9, and that the binding site involves residues highly, conserved across FHA domains. The results, along with other recent, reports, suggest that FHA domains could have pTyr and pSer/Thr dual, specificity.
+<StructureSection load='1qu5' size='340' side='right'caption='[[1qu5]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1qu5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QU5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QU5 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1qu5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qu5 OCA], [https://pdbe.org/1qu5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qu5 RCSB], [https://www.ebi.ac.uk/pdbsum/1qu5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qu5 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/RAD53_YEAST RAD53_YEAST] Controls S-phase checkpoint as well as G1 and G2 DNA damage checkpoints. Phosphorylates proteins on serine, threonine, and tyrosine. Prevents entry into anaphase and mitotic exit after DNA damage via regulation of the Polo kinase CDC5. Seems to be involved in the phosphorylation of RPH1.<ref>PMID:8355715</ref> <ref>PMID:7958905</ref> <ref>PMID:10550056</ref> <ref>PMID:11809875</ref> <ref>PMID:15024067</ref>
+== 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/qu/1qu5_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=1qu5 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The forkhead-associated (FHA) domain is a 55-75 amino acid residue module found in &gt;20 proteins from yeast to human. It has been suggested to participate in signal transduction pathways, perhaps via protein-protein interactions involving recognition of phosphopeptides. Neither the structure nor the ligand of FHA is known. Yeast Rad53, a checkpoint protein involved in DNA damage response, contains two FHA domains, FHA1 (residues 66-116) and FHA2 (residues 601-664), the second of which recognizes phosphorylated Rad9. We herein report the solution structure of an "FHA2-containing domain" of Rad53 (residues 573-730). The structure consists of a beta-sandwich containing two antiparallel beta-sheets and a short, C-terminal alpha-helix. Binding experiments suggested that the FHA2-containing domain specifically recognizes pTyr and a pTyr-containing peptide from Rad9, and that the binding site involves residues highly conserved across FHA domains. The results, along with other recent reports, suggest that FHA domains could have pTyr and pSer/Thr dual specificity.
-==About this Structure==
+Structure and function of a new phosphopeptide-binding domain containing the FHA2 of Rad53.,Liao H, Byeon IJ, Tsai MD J Mol Biol. 1999 Dec 10;294(4):1041-9. PMID:10588905<ref>PMID:10588905</ref>
-QU5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QU5 OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-Structure and function of a new phosphopeptide-binding domain containing the FHA2 of Rad53., Liao H, Byeon IJ, Tsai MD, J Mol Biol. 1999 Dec 10;294(4):1041-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10588905 10588905]
+</div>
-[[Category: Saccharomyces cerevisiae]]
+<div class="pdbe-citations 1qu5" style="background-color:#fffaf0;"></div>
-[[Category: Single protein]]
-[[Category: Byeon, I.J.L.]]
-[[Category: Liao, H.]]
-[[Category: Tsai, M.D.]]
-[[Category: fha]]
-[[Category: rad53]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:59:23 2007''
+==See Also==
+*[[Protein kinase Spk1|Protein kinase Spk1]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Saccharomyces cerevisiae]]
+[[Category: Byeon I-JL]]
+[[Category: Liao H]]
+[[Category: Tsai M-D]]

1qu5

From Proteopedia

Current revision

NMR STRUCTURE OF A NEW PHOSPHOTYROSINE BINDING DOMAIN CONTAINING THE FHA2 DOMAIN OF RAD 53

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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