5iqz

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of N-terminal domain of Human SIRT7

Structural highlights

5iqz is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.334Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MALE_ECOLI Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.SIR7_HUMAN NAD-dependent protein deacetylase that specifically mediates deacetylation of histone H3 at 'Lys-18' (H3K18Ac). In contrast to other histone deacetylases, displays selectivity for a single histone mark, H3K18Ac, directly linked to control of gene expression. H3K18Ac is mainly present around the transcription start site of genes and has been linked to activation of nuclear hormone receptors. SIRT7 thereby acts as a transcription repressor. Moreover, H3K18 hypoacetylation has been reported as a marker of malignancy in various cancers and seems to maintain the transformed phenotype of cancer cells. These data suggest that SIRT7 may play a key role in oncogenic transformation by suppresses expression of tumor suppressor genes by locus-specific deacetylation of H3K18Ac at promoter regions. Also required to restore the transcription of ribosomal RNA (rRNA) at the exit from mitosis: promotes the association of RNA polymerase I with the rDNA promoter region and coding region. Stimulates transcription activity of the RNA polymerase I complex. May also deacetylate p53/TP53 and promotes cell survival, however such data need additional confirmation.^[1] ^[2] ^[3]

Publication Abstract from PubMed

Human SIRT7 is an NAD+ dependent deacetylase which belongs to sirtuin family of proteins. SIRT7, like other sirtuins has conserved catalytic domain and is flanked by N- and C- terminal domains reported to play vital functional roles. Here, we report the crystal structure of the N-terminal domain of human SIRT7 (SIRT7NTD ) at 2.3 A resolution as MBP-SIRT7NTD fusion protein. SIRT7NTD adopts three-helical domain architecture and comparative structural analyses suggest similarities to some DNA binding motifs and transcription regulators. We also report here the importance of N- and C-terminal domains in soluble expression of SIRT7. This article is protected by copyright. All rights reserved.

Crystal structure of the N-terminal domain of human SIRT7 reveals a three-helical domain architecture.,Priyanka A, Solanki V, Parkesh R, Thakur KG Proteins. 2016 Jun 10. doi: 10.1002/prot.25085. PMID:27287224^[4]

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

References

↑ Ford E, Voit R, Liszt G, Magin C, Grummt I, Guarente L. Mammalian Sir2 homolog SIRT7 is an activator of RNA polymerase I transcription. Genes Dev. 2006 May 1;20(9):1075-80. doi: 10.1101/gad.1399706. Epub 2006 Apr 17. PMID:16618798 doi:http://dx.doi.org/10.1101/gad.1399706
↑ Grob A, Roussel P, Wright JE, McStay B, Hernandez-Verdun D, Sirri V. Involvement of SIRT7 in resumption of rDNA transcription at the exit from mitosis. J Cell Sci. 2009 Feb 15;122(Pt 4):489-98. doi: 10.1242/jcs.042382. Epub 2009 Jan , 27. PMID:19174463 doi:http://dx.doi.org/10.1242/jcs.042382
↑ Barber MF, Michishita-Kioi E, Xi Y, Tasselli L, Kioi M, Moqtaderi Z, Tennen RI, Paredes S, Young NL, Chen K, Struhl K, Garcia BA, Gozani O, Li W, Chua KF. SIRT7 links H3K18 deacetylation to maintenance of oncogenic transformation. Nature. 2012 Jul 5;487(7405):114-8. doi: 10.1038/nature11043. PMID:22722849 doi:http://dx.doi.org/10.1038/nature11043
↑ Priyanka A, Solanki V, Parkesh R, Thakur KG. Crystal structure of the N-terminal domain of human SIRT7 reveals a three-helical domain architecture. Proteins. 2016 Jun 10. doi: 10.1002/prot.25085. PMID:27287224 doi:http://dx.doi.org/10.1002/prot.25085

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5iqz"

Categories: Homo sapiens | Large Structures | Priyanka A | Thakur KG

@@ Line 1: / Line 1: @@
 ==Crystal structure of N-terminal domain of Human SIRT7==
-<StructureSection load='5iqz' size='340' side='right' caption='[[5iqz]], [[Resolution|resolution]] 2.33&Aring;' scene=''>
+<StructureSection load='5iqz' size='340' side='right'caption='[[5iqz]], [[Resolution|resolution]] 2.33&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5iqz]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IQZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IQZ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5iqz]] is a 1 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=5IQZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IQZ FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MAL:MALTOSE'>MAL</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.334&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5iqz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5iqz OCA], [http://pdbe.org/5iqz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5iqz RCSB], [http://www.ebi.ac.uk/pdbsum/5iqz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5iqz ProSAT]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</scene></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=5iqz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5iqz OCA], [https://pdbe.org/5iqz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5iqz RCSB], [https://www.ebi.ac.uk/pdbsum/5iqz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5iqz ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.[https://www.uniprot.org/uniprot/SIR7_HUMAN SIR7_HUMAN] NAD-dependent protein deacetylase that specifically mediates deacetylation of histone H3 at 'Lys-18' (H3K18Ac). In contrast to other histone deacetylases, displays selectivity for a single histone mark, H3K18Ac, directly linked to control of gene expression. H3K18Ac is mainly present around the transcription start site of genes and has been linked to activation of nuclear hormone receptors. SIRT7 thereby acts as a transcription repressor. Moreover, H3K18 hypoacetylation has been reported as a marker of malignancy in various cancers and seems to maintain the transformed phenotype of cancer cells. These data suggest that SIRT7 may play a key role in oncogenic transformation by suppresses expression of tumor suppressor genes by locus-specific deacetylation of H3K18Ac at promoter regions. Also required to restore the transcription of ribosomal RNA (rRNA) at the exit from mitosis: promotes the association of RNA polymerase I with the rDNA promoter region and coding region. Stimulates transcription activity of the RNA polymerase I complex. May also deacetylate p53/TP53 and promotes cell survival, however such data need additional confirmation.<ref>PMID:16618798</ref> <ref>PMID:19174463</ref> <ref>PMID:22722849</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 16: / Line 19: @@
 </div>
 <div class="pdbe-citations 5iqz" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Histone deacetylase 3D structures|Histone deacetylase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Priyanka, A]]
+[[Category: Homo sapiens]]
-[[Category: Thakur, K G]]
+[[Category: Large Structures]]
-[[Category: Alpha histone deacetylase sirtuin]]
+[[Category: Priyanka A]]
-[[Category: Fusion protein]]
+[[Category: Thakur KG]]
-[[Category: Maltose binding]]
-[[Category: Sirt7]]
-[[Category: Sugar binding protein]]

5iqz

From Proteopedia

Current revision

Crystal structure of N-terminal domain of Human SIRT7

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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