5ums

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of middle double PH domain of human FACT complex subunit SSRP1

Structural highlights

5ums 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 1.569Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SSRP1_HUMAN Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. The FACT complex is probably also involved in phosphorylation of 'Ser-392' of p53/TP53 via its association with CK2 (casein kinase II). Binds specifically to double-stranded DNA and at low levels to DNA modified by the antitumor agent cisplatin. May potentiate cisplatin-induced cell death by blocking replication and repair of modified DNA. Also acts as a transcriptional coactivator for p63/TP63.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] ^[8]

References

↑ Orphanides G, LeRoy G, Chang CH, Luse DS, Reinberg D. FACT, a factor that facilitates transcript elongation through nucleosomes. Cell. 1998 Jan 9;92(1):105-16. PMID:9489704
↑ Dyer MA, Hayes PJ, Baron MH. The HMG domain protein SSRP1/PREIIBF is involved in activation of the human embryonic beta-like globin gene. Mol Cell Biol. 1998 May;18(5):2617-28. PMID:9566881
↑ LeRoy G, Orphanides G, Lane WS, Reinberg D. Requirement of RSF and FACT for transcription of chromatin templates in vitro. Science. 1998 Dec 4;282(5395):1900-4. PMID:9836642
↑ Wada T, Orphanides G, Hasegawa J, Kim DK, Shima D, Yamaguchi Y, Fukuda A, Hisatake K, Oh S, Reinberg D, Handa H. FACT relieves DSIF/NELF-mediated inhibition of transcriptional elongation and reveals functional differences between P-TEFb and TFIIH. Mol Cell. 2000 Jun;5(6):1067-72. PMID:10912001
↑ Keller DM, Zeng X, Wang Y, Zhang QH, Kapoor M, Shu H, Goodman R, Lozano G, Zhao Y, Lu H. A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16, and SSRP1. Mol Cell. 2001 Feb;7(2):283-92. PMID:11239457
↑ Zeng SX, Dai MS, Keller DM, Lu H. SSRP1 functions as a co-activator of the transcriptional activator p63. EMBO J. 2002 Oct 15;21(20):5487-97. PMID:12374749
↑ Belotserkovskaya R, Oh S, Bondarenko VA, Orphanides G, Studitsky VM, Reinberg D. FACT facilitates transcription-dependent nucleosome alteration. Science. 2003 Aug 22;301(5636):1090-3. PMID:12934006 doi:http://dx.doi.org/10.1126/science.1085703
↑ Pavri R, Zhu B, Li G, Trojer P, Mandal S, Shilatifard A, Reinberg D. Histone H2B monoubiquitination functions cooperatively with FACT to regulate elongation by RNA polymerase II. Cell. 2006 May 19;125(4):703-17. PMID:16713563 doi:http://dx.doi.org/S0092-8674(06)00570-8

1 Structural highlights
2 Function
3 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 3: / Line 3: @@
 <StructureSection load='5ums' size='340' side='right'caption='[[5ums]], [[Resolution|resolution]] 1.57&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5ums]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UMS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UMS FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5ums]] 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=5UMS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UMS FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5umr|5umr]], [[5umt|5umt]], [[5umu|5umu]], [[5umv|5umv]]</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]] 1.569&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SSRP1, FACT80 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5ums FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ums OCA], [https://pdbe.org/5ums PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ums RCSB], [https://www.ebi.ac.uk/pdbsum/5ums PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ums ProSAT]</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=5ums FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ums OCA], [http://pdbe.org/5ums PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ums RCSB], [http://www.ebi.ac.uk/pdbsum/5ums PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ums ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/SSRP1_HUMAN SSRP1_HUMAN]] Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. The FACT complex is probably also involved in phosphorylation of 'Ser-392' of p53/TP53 via its association with CK2 (casein kinase II). Binds specifically to double-stranded DNA and at low levels to DNA modified by the antitumor agent cisplatin. May potentiate cisplatin-induced cell death by blocking replication and repair of modified DNA. Also acts as a transcriptional coactivator for p63/TP63.<ref>PMID:9489704</ref> <ref>PMID:9566881</ref> <ref>PMID:9836642</ref> <ref>PMID:10912001</ref> <ref>PMID:11239457</ref> <ref>PMID:12374749</ref> <ref>PMID:12934006</ref> <ref>PMID:16713563</ref>
+[https://www.uniprot.org/uniprot/SSRP1_HUMAN SSRP1_HUMAN] Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. The FACT complex is probably also involved in phosphorylation of 'Ser-392' of p53/TP53 via its association with CK2 (casein kinase II). Binds specifically to double-stranded DNA and at low levels to DNA modified by the antitumor agent cisplatin. May potentiate cisplatin-induced cell death by blocking replication and repair of modified DNA. Also acts as a transcriptional coactivator for p63/TP63.<ref>PMID:9489704</ref> <ref>PMID:9566881</ref> <ref>PMID:9836642</ref> <ref>PMID:10912001</ref> <ref>PMID:11239457</ref> <ref>PMID:12374749</ref> <ref>PMID:12934006</ref> <ref>PMID:16713563</ref>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Botuyan, M V]]
+[[Category: Botuyan MV]]
-[[Category: Hu, Q]]
+[[Category: Hu Q]]
-[[Category: Mer, G]]
+[[Category: Mer G]]
-[[Category: Su, D]]
+[[Category: Su D]]
-[[Category: Thompson, J R]]
+[[Category: Thompson JR]]
-[[Category: Double ph domain]]
-[[Category: Fact]]
-[[Category: Histone chaperone]]
-[[Category: Transcription]]

5ums

From Proteopedia

Current revision

Crystal structure of middle double PH domain of human FACT complex subunit SSRP1

Structural highlights

Function

References

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Proteopedia Page Contributors and Editors (what is this?)

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