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[[Image:2hwy.gif|left|200px]]
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{{STRUCTURE_2hwy|  PDB=2hwy  |  SCENE=  }}
'''Structure of PIN domain of human SMG5.'''


==Structure of PIN domain of human SMG5.==
<StructureSection load='2hwy' size='340' side='right'caption='[[2hwy]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2hwy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HWY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HWY 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]] 2.75&#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=2hwy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hwy OCA], [https://pdbe.org/2hwy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hwy RCSB], [https://www.ebi.ac.uk/pdbsum/2hwy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hwy ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SMG5_HUMAN SMG5_HUMAN] Plays a role in nonsense-mediated mRNA decay. Does not have RNase activity by itself. Promotes dephosphorylation of UPF1. Together with SMG7 is thought to provide a link to the mRNA degradation machinery involving exonucleolytic pathways, and to serve as an adapter for UPF1 to protein phosphatase 2A (PP2A), thereby triggering UPF1 dephosphorylation. Necessary for TERT activity.<ref>PMID:17053788</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/hw/2hwy_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=2hwy ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
SMG6 and SMG5 are essential factors in nonsense-mediated mRNA decay, a conserved pathway that degrades mRNAs with premature translation termination codons. Both SMG5 and SMG6 have been predicted to contain a C-terminal PIN (PilT N-terminus) domain, present in proteins with ribonuclease activity. We have determined the structures of human SMG5 and SMG6 PIN domains. Although they share a similar overall fold related to ribonucleases of the RNase H family, they have local differences at the putative active site. SMG6 has the canonical triad of acidic residues that are crucial in RNase H for nuclease activity, while SMG5 lacks key catalytic residues. The structural differences are reflected at the functional level. Only the PIN domain of SMG6 has degradation activity on single-stranded RNA in vitro. This difference in catalytic activity is conserved in Drosophila, where an SMG6 with an inactive PIN domain inhibits NMD in a dominant-negative manner. Our findings suggest that the NMD machinery has intrinsic nuclease activity that is likely to contribute to the rapid decay of mRNAs that terminate translation prematurely.


==Overview==
Structures of the PIN domains of SMG6 and SMG5 reveal a nuclease within the mRNA surveillance complex.,Glavan F, Behm-Ansmant I, Izaurralde E, Conti E EMBO J. 2006 Nov 1;25(21):5117-25. Epub 2006 Oct 19. PMID:17053788<ref>PMID:17053788</ref>
SMG6 and SMG5 are essential factors in nonsense-mediated mRNA decay, a conserved pathway that degrades mRNAs with premature translation termination codons. Both SMG5 and SMG6 have been predicted to contain a C-terminal PIN (PilT N-terminus) domain, present in proteins with ribonuclease activity. We have determined the structures of human SMG5 and SMG6 PIN domains. Although they share a similar overall fold related to ribonucleases of the RNase H family, they have local differences at the putative active site. SMG6 has the canonical triad of acidic residues that are crucial in RNase H for nuclease activity, while SMG5 lacks key catalytic residues. The structural differences are reflected at the functional level. Only the PIN domain of SMG6 has degradation activity on single-stranded RNA in vitro. This difference in catalytic activity is conserved in Drosophila, where an SMG6 with an inactive PIN domain inhibits NMD in a dominant-negative manner. Our findings suggest that the NMD machinery has intrinsic nuclease activity that is likely to contribute to the rapid decay of mRNAs that terminate translation prematurely.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2HWY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HWY OCA].
</div>
<div class="pdbe-citations 2hwy" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Structures of the PIN domains of SMG6 and SMG5 reveal a nuclease within the mRNA surveillance complex., Glavan F, Behm-Ansmant I, Izaurralde E, Conti E, EMBO J. 2006 Nov 1;25(21):5117-25. Epub 2006 Oct 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17053788 17053788]
*[[Serine/threonine protein kinase 3D structures|Serine/threonine protein kinase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Behm-Ansmant, I.]]
[[Category: Behm-Ansmant I]]
[[Category: Conti, E.]]
[[Category: Conti E]]
[[Category: Glavan, F.]]
[[Category: Glavan F]]
[[Category: Izaurralde, E.]]
[[Category: Izaurralde E]]
[[Category: Decay]]
[[Category: Est1a]]
[[Category: Nmd]]
[[Category: P body]]
[[Category: Rna degradation]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 06:48:48 2008''

Latest revision as of 10:02, 30 August 2023

Structure of PIN domain of human SMG5.

2hwy, resolution 2.75Å

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