6bx3

From Proteopedia

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Revision as of 09:56, 4 December 2019

Structure of histone H3k4 methyltransferase

Structural highlights

6bx3 is a 7 chain structure with sequence from Baker's yeast. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	SET1, SCY_2511 (Baker's yeast), BRE2, CPS60, YLR015W (Baker's yeast), SDC1, CPS25, SAF19, YDR469W (Baker's yeast), SPP1, CPS40, SAF41, YPL138C (Baker's yeast), SWD1, CPS50, SAF49, YAR003W, FUN16 (Baker's yeast), SWD3, CPS30, SAF35, YBR175W, YBR1237 (Baker's yeast)
Activity:	Histone-lysine N-methyltransferase, with EC number 2.1.1.43
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SWD3_YEAST] The COMPASS (Set1C) complex specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation.^[1] ^[2] [SPP1_YEAST] The COMPASS (Set1C) complex specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation.^[3] ^[4] [A6ZT27_YEAS7] Catalytic component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation.[PIRNR:PIRNR037104] [SDC1_YEAST] The COMPASS (Set1C) complex specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently activates gene expression by regulating transcription elongation and plays a role in telomere length maintenance.^[5] ^[6] [BRE2_YEAST] The COMPASS (Set1C) complex specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation.^[7] ^[8] [SWD1_YEAST] The COMPASS (Set1C) complex specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation.^[9] ^[10]

Publication Abstract from PubMed

The methylation of histone 3 lysine 4 (H3K4) is carried out by an evolutionarily conserved family of methyltransferases referred to as complex of proteins associated with Set1 (COMPASS). The activity of the catalytic SET domain (su(var)3-9, enhancer-of-zeste, and trithorax) is endowed through forming a complex with a set of core proteins that are widely shared from yeast to humans. We obtained cryo-electron microscopy (cryo-EM) maps of the yeast Set1/COMPASS core complex at overall 4.0- to 4.4-A resolution, providing insights into its structural organization and conformational dynamics. The Cps50 C-terminal tail weaves within the complex to provide a central scaffold for assembly. The SET domain, snugly positioned at the junction of the Y-shaped complex, is extensively contacted by Cps60 (Bre2), Cps50 (Swd1), and Cps30 (Swd3). The mobile SET-I motif of the SET domain is engaged by Cps30, explaining its key role in COMPASS catalytic activity toward higher H3K4 methylation states.

Structure and Conformational Dynamics of a COMPASS Histone H3K4 Methyltransferase Complex.,Qu Q, Takahashi YH, Yang Y, Hu H, Zhang Y, Brunzelle JS, Couture JF, Shilatifard A, Skiniotis G Cell. 2018 Aug 23;174(5):1117-1126.e12. doi: 10.1016/j.cell.2018.07.020. Epub, 2018 Aug 9. PMID:30100186^[11]

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

References

↑ Roguev A, Schaft D, Shevchenko A, Pijnappel WW, Wilm M, Aasland R, Stewart AF. The Saccharomyces cerevisiae Set1 complex includes an Ash2 homologue and methylates histone 3 lysine 4. EMBO J. 2001 Dec 17;20(24):7137-48. PMID:11742990 doi:http://dx.doi.org/10.1093/emboj/20.24.7137
↑ Krogan NJ, Dover J, Khorrami S, Greenblatt JF, Schneider J, Johnston M, Shilatifard A. COMPASS, a histone H3 (Lysine 4) methyltransferase required for telomeric silencing of gene expression. J Biol Chem. 2002 Mar 29;277(13):10753-5. Epub 2002 Jan 22. PMID:11805083 doi:http://dx.doi.org/10.1074/jbc.C200023200
↑ Roguev A, Schaft D, Shevchenko A, Pijnappel WW, Wilm M, Aasland R, Stewart AF. The Saccharomyces cerevisiae Set1 complex includes an Ash2 homologue and methylates histone 3 lysine 4. EMBO J. 2001 Dec 17;20(24):7137-48. PMID:11742990 doi:http://dx.doi.org/10.1093/emboj/20.24.7137
↑ Krogan NJ, Dover J, Khorrami S, Greenblatt JF, Schneider J, Johnston M, Shilatifard A. COMPASS, a histone H3 (Lysine 4) methyltransferase required for telomeric silencing of gene expression. J Biol Chem. 2002 Mar 29;277(13):10753-5. Epub 2002 Jan 22. PMID:11805083 doi:http://dx.doi.org/10.1074/jbc.C200023200
↑ Roguev A, Schaft D, Shevchenko A, Pijnappel WW, Wilm M, Aasland R, Stewart AF. The Saccharomyces cerevisiae Set1 complex includes an Ash2 homologue and methylates histone 3 lysine 4. EMBO J. 2001 Dec 17;20(24):7137-48. PMID:11742990 doi:http://dx.doi.org/10.1093/emboj/20.24.7137
↑ Krogan NJ, Dover J, Khorrami S, Greenblatt JF, Schneider J, Johnston M, Shilatifard A. COMPASS, a histone H3 (Lysine 4) methyltransferase required for telomeric silencing of gene expression. J Biol Chem. 2002 Mar 29;277(13):10753-5. Epub 2002 Jan 22. PMID:11805083 doi:http://dx.doi.org/10.1074/jbc.C200023200
↑ Roguev A, Schaft D, Shevchenko A, Pijnappel WW, Wilm M, Aasland R, Stewart AF. The Saccharomyces cerevisiae Set1 complex includes an Ash2 homologue and methylates histone 3 lysine 4. EMBO J. 2001 Dec 17;20(24):7137-48. PMID:11742990 doi:http://dx.doi.org/10.1093/emboj/20.24.7137
↑ Krogan NJ, Dover J, Khorrami S, Greenblatt JF, Schneider J, Johnston M, Shilatifard A. COMPASS, a histone H3 (Lysine 4) methyltransferase required for telomeric silencing of gene expression. J Biol Chem. 2002 Mar 29;277(13):10753-5. Epub 2002 Jan 22. PMID:11805083 doi:http://dx.doi.org/10.1074/jbc.C200023200
↑ Roguev A, Schaft D, Shevchenko A, Pijnappel WW, Wilm M, Aasland R, Stewart AF. The Saccharomyces cerevisiae Set1 complex includes an Ash2 homologue and methylates histone 3 lysine 4. EMBO J. 2001 Dec 17;20(24):7137-48. PMID:11742990 doi:http://dx.doi.org/10.1093/emboj/20.24.7137
↑ Krogan NJ, Dover J, Khorrami S, Greenblatt JF, Schneider J, Johnston M, Shilatifard A. COMPASS, a histone H3 (Lysine 4) methyltransferase required for telomeric silencing of gene expression. J Biol Chem. 2002 Mar 29;277(13):10753-5. Epub 2002 Jan 22. PMID:11805083 doi:http://dx.doi.org/10.1074/jbc.C200023200
↑ Qu Q, Takahashi YH, Yang Y, Hu H, Zhang Y, Brunzelle JS, Couture JF, Shilatifard A, Skiniotis G. Structure and Conformational Dynamics of a COMPASS Histone H3K4 Methyltransferase Complex. Cell. 2018 Aug 23;174(5):1117-1126.e12. doi: 10.1016/j.cell.2018.07.020. Epub, 2018 Aug 9. PMID:30100186 doi:http://dx.doi.org/10.1016/j.cell.2018.07.020

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6bx3"

@@ Line 1: / Line 1: @@
 ==Structure of histone H3k4 methyltransferase==
-<StructureSection load='6bx3' size='340' side='right' caption='[[6bx3]], [[Resolution|resolution]] 4.30&Aring;' scene=''>
+<StructureSection load='6bx3' size='340' side='right'caption='[[6bx3]], [[Resolution|resolution]] 4.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6bx3]] is a 7 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BX3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BX3 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6bx3]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BX3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BX3 FirstGlance]. <br>
-</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] </span></td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SET1, SCY_2511 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=307796 Baker's yeast]), BRE2, CPS60, YLR015W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), SDC1, CPS25, SAF19, YDR469W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), SPP1, CPS40, SAF41, YPL138C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), SWD1, CPS50, SAF49, YAR003W, FUN16 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), SWD3, CPS30, SAF35, YBR175W, YBR1237 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] </span></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=6bx3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bx3 OCA], [http://pdbe.org/6bx3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bx3 RCSB], [http://www.ebi.ac.uk/pdbsum/6bx3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bx3 ProSAT]</span></td></tr>
 </table>
@@ Line 22: / Line 23: @@
 __TOC__
 </StructureSection>
+[[Category: Baker's yeast]]
 [[Category: Histone-lysine N-methyltransferase]]
+[[Category: Large Structures]]
 [[Category: Qu, Q H]]
 [[Category: Skiniotis, G]]
 [[Category: Gene regulation-transferase complex]]
 [[Category: Histone h3k4 methyltransferase]]

6bx3

From Proteopedia

Revision as of 09:56, 4 December 2019

Structure of histone H3k4 methyltransferase

Structural highlights

Function

Publication Abstract from PubMed

References

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