10gx: Difference between revisions

Latest revision as of 16:00, 22 July 2026

Yeast Blm10 apo Structure

Structural highlights

10gx is a 1 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 3.2Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

BLM10_YEAST Associated component of the proteasome that specifically recognizes acetylated histones and promotes ATP- and ubiquitin-independent degradation of core histones during DNA damage response. Recognizes and binds acetylated histones via its bromodomain-like (BRDL) region and activates the proteasome by opening the gated channel for substrate entry. Binds to the core proteasome via its C-terminus, which occupies the same binding sites as the proteasomal ATPases, opening the closed structure of the proteasome via an active gating mechanism. Involved in DNA damage response in somatic cells: binds to acetylated histones and promotes degradation of histones following DNA double-strand breaks.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7]

References

↑ Febres DE, Pramanik A, Caton M, Doherty K, McKoy J, Garcia E, Alejo W, Moore CW. The novel BLM3 gene encodes a protein that protects against lethal effects of oxidative damage. Cell Mol Biol (Noisy-le-grand). 2001 Nov;47(7):1149-62. PMID:11842813
↑ Fehlker M, Wendler P, Lehmann A, Enenkel C. Blm3 is part of nascent proteasomes and is involved in a late stage of nuclear proteasome assembly. EMBO Rep. 2003 Oct;4(10):959-63. Epub 2003 Sep 12. PMID:12973301 doi:https://dx.doi.org/10.1038/sj.embor.embor938
↑ Schmidt M, Haas W, Crosas B, Santamaria PG, Gygi SP, Walz T, Finley D. The HEAT repeat protein Blm10 regulates the yeast proteasome by capping the core particle. Nat Struct Mol Biol. 2005 Apr;12(4):294-303. Epub 2005 Mar 20. PMID:15778719 doi:https://dx.doi.org/nsmb914
↑ Lehmann A, Jechow K, Enenkel C. Blm10 binds to pre-activated proteasome core particles with open gate conformation. EMBO Rep. 2008 Dec;9(12):1237-43. doi: 10.1038/embor.2008.190. Epub 2008 Oct 17. PMID:18927584 doi:https://dx.doi.org/10.1038/embor.2008.190
↑ Sadre-Bazzaz K, Whitby FG, Robinson H, Formosa T, Hill CP. Structure of a Blm10 complex reveals common mechanisms for proteasome binding and gate opening. Mol Cell. 2010 Mar 12;37(5):728-35. PMID:20227375 doi:10.1016/j.molcel.2010.02.002
↑ Dange T, Smith D, Noy T, Rommel PC, Jurzitza L, Cordero RJ, Legendre A, Finley D, Goldberg AL, Schmidt M. Blm10 protein promotes proteasomal substrate turnover by an active gating mechanism. J Biol Chem. 2011 Dec 16;286(50):42830-9. doi: 10.1074/jbc.M111.300178. Epub 2011, Oct 24. PMID:22025621 doi:https://dx.doi.org/10.1074/jbc.M111.300178
↑ Qian MX, Pang Y, Liu CH, Haratake K, Du BY, Ji DY, Wang GF, Zhu QQ, Song W, Yu Y, Zhang XX, Huang HT, Miao S, Chen LB, Zhang ZH, Liang YN, Liu S, Cha H, Yang D, Zhai Y, Komatsu T, Tsuruta F, Li H, Cao C, Li W, Li GH, Cheng Y, Chiba T, Wang L, Goldberg AL, Shen Y, Qiu XB. Acetylation-mediated proteasomal degradation of core histones during DNA repair and spermatogenesis. Cell. 2013 May 23;153(5):1012-24. doi: 10.1016/j.cell.2013.04.032. PMID:23706739 doi:https://dx.doi.org/10.1016/j.cell.2013.04.032

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Febres DE, Pramanik A, Caton M, Doherty K, McKoy J, Garcia E, Alejo W, Moore CW. The novel BLM3 gene encodes a protein that protects against lethal effects of oxidative damage. Cell Mol Biol (Noisy-le-grand). 2001 Nov;47(7):1149-62. PMID:11842813

[2] Fehlker M, Wendler P, Lehmann A, Enenkel C. Blm3 is part of nascent proteasomes and is involved in a late stage of nuclear proteasome assembly. EMBO Rep. 2003 Oct;4(10):959-63. Epub 2003 Sep 12. PMID:12973301 doi:https://dx.doi.org/10.1038/sj.embor.embor938

[3] Schmidt M, Haas W, Crosas B, Santamaria PG, Gygi SP, Walz T, Finley D. The HEAT repeat protein Blm10 regulates the yeast proteasome by capping the core particle. Nat Struct Mol Biol. 2005 Apr;12(4):294-303. Epub 2005 Mar 20. PMID:15778719 doi:https://dx.doi.org/nsmb914

[4] Lehmann A, Jechow K, Enenkel C. Blm10 binds to pre-activated proteasome core particles with open gate conformation. EMBO Rep. 2008 Dec;9(12):1237-43. doi: 10.1038/embor.2008.190. Epub 2008 Oct 17. PMID:18927584 doi:https://dx.doi.org/10.1038/embor.2008.190

[5] Sadre-Bazzaz K, Whitby FG, Robinson H, Formosa T, Hill CP. Structure of a Blm10 complex reveals common mechanisms for proteasome binding and gate opening. Mol Cell. 2010 Mar 12;37(5):728-35. PMID:20227375 doi:10.1016/j.molcel.2010.02.002

[6] Dange T, Smith D, Noy T, Rommel PC, Jurzitza L, Cordero RJ, Legendre A, Finley D, Goldberg AL, Schmidt M. Blm10 protein promotes proteasomal substrate turnover by an active gating mechanism. J Biol Chem. 2011 Dec 16;286(50):42830-9. doi: 10.1074/jbc.M111.300178. Epub 2011, Oct 24. PMID:22025621 doi:https://dx.doi.org/10.1074/jbc.M111.300178

[7] Qian MX, Pang Y, Liu CH, Haratake K, Du BY, Ji DY, Wang GF, Zhu QQ, Song W, Yu Y, Zhang XX, Huang HT, Miao S, Chen LB, Zhang ZH, Liang YN, Liu S, Cha H, Yang D, Zhai Y, Komatsu T, Tsuruta F, Li H, Cao C, Li W, Li GH, Cheng Y, Chiba T, Wang L, Goldberg AL, Shen Y, Qiu XB. Acetylation-mediated proteasomal degradation of core histones during DNA repair and spermatogenesis. Cell. 2013 May 23;153(5):1012-24. doi: 10.1016/j.cell.2013.04.032. PMID:23706739 doi:https://dx.doi.org/10.1016/j.cell.2013.04.032

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 10gx is ON HOLD
+==Yeast Blm10 apo Structure==
+<StructureSection load='10gx' size='340' side='right'caption='[[10gx]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
-Authors:
+== Structural highlights ==
+<table><tr><td colspan='2'>[[10gx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=10GX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=10GX FirstGlance]. <br>
-Description:
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.2&#8491;</td></tr>
-[[Category: Unreleased Structures]]
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=10gx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=10gx OCA], [https://pdbe.org/10gx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=10gx RCSB], [https://www.ebi.ac.uk/pdbsum/10gx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=10gx ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/BLM10_YEAST BLM10_YEAST] Associated component of the proteasome that specifically recognizes acetylated histones and promotes ATP- and ubiquitin-independent degradation of core histones during DNA damage response. Recognizes and binds acetylated histones via its bromodomain-like (BRDL) region and activates the proteasome by opening the gated channel for substrate entry. Binds to the core proteasome via its C-terminus, which occupies the same binding sites as the proteasomal ATPases, opening the closed structure of the proteasome via an active gating mechanism. Involved in DNA damage response in somatic cells: binds to acetylated histones and promotes degradation of histones following DNA double-strand breaks.<ref>PMID:11842813</ref> <ref>PMID:12973301</ref> <ref>PMID:15778719</ref> <ref>PMID:18927584</ref> <ref>PMID:20227375</ref> <ref>PMID:22025621</ref> <ref>PMID:23706739</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Saccharomyces cerevisiae S288C]]
+[[Category: Fermin Perez E]]
+[[Category: Hanna J]]
+[[Category: Rawson S]]
+[[Category: Venclovaite U]]
+[[Category: Walsh Jr RM]]

10gx: Difference between revisions

Latest revision as of 16:00, 22 July 2026

Yeast Blm10 apo Structure

Structural highlights

Function

References

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