3mp1: Difference between revisions

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-[[Image:3mp1.jpg|left|200px]]
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+==Complex structure of Sgf29 and trimethylated H3K4==
-The line below this paragraph, containing "STRUCTURE_3mp1", creates the "Structure Box" on the page.
+<StructureSection load='3mp1' size='340' side='right'caption='[[3mp1]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3mp1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12], [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C], [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct] and [https://en.wikipedia.org/wiki/Unidentified Unidentified]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MP1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MP1 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=M3L:N-TRIMETHYLLYSINE'>M3L</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</scene></td></tr>
-{{STRUCTURE_3mp1|  PDB=3mp1  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3mp1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mp1 OCA], [https://pdbe.org/3mp1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mp1 RCSB], [https://www.ebi.ac.uk/pdbsum/3mp1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mp1 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/SGF29_YEAST SGF29_YEAST] Chromatin reader component of the transcription regulatory histone acetylation (HAT) complexes SAGA and SLIK (PubMed:10026213, PubMed:15647753, PubMed:21685874, PubMed:24307402). In the SAGA complex, SGF29 specifically recognizes and binds methylated 'Lys-4' of histone H3 (H3K4me), with a preference for trimethylated form (H3K4me3) (PubMed:21685874). SGF29 is also required for heterochromatin boundary formation function (PubMed:24307402). SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes At the promoters, SAGA is required for recruitment of the basal transcription machinery (PubMed:10026213). It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8) (PubMed:10026213). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs) (PubMed:10026213). SLIK is proposed to have partly overlapping functions with SAGA (PubMed:15647753). It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus (PubMed:15647753).<ref>PMID:10026213</ref> <ref>PMID:15647753</ref> <ref>PMID:21685874</ref> <ref>PMID:24307402</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The SAGA (Spt-Ada-Gcn5 acetyltransferase) complex is an important chromatin modifying complex that can both acetylate and deubiquitinate histones. Sgf29 is a novel component of the SAGA complex. Here, we report the crystal structures of the tandem Tudor domains of Saccharomyces cerevisiae and human Sgf29 and their complexes with H3K4me2 and H3K4me3 peptides, respectively, and show that Sgf29 selectively binds H3K4me2/3 marks. Our crystal structures reveal that Sgf29 harbours unique tandem Tudor domains in its C-terminus. The tandem Tudor domains in Sgf29 tightly pack against each other face-to-face with each Tudor domain harbouring a negatively charged pocket accommodating the first residue alanine and methylated K4 residue of histone H3, respectively. The H3A1 and K4me3 binding pockets and the limited binding cleft length between these two binding pockets are the structural determinants in conferring the ability of Sgf29 to selectively recognize H3K4me2/3. Our in vitro and in vivo functional assays show that Sgf29 recognizes methylated H3K4 to recruit the SAGA complex to its targets sites and mediates histone H3 acetylation, underscoring the importance of Sgf29 in gene regulation.
-===Complex structure of Sgf29 and trimethylated H3K4===
+Sgf29 binds histone H3K4me2/3 and is required for SAGA complex recruitment and histone H3 acetylation.,Bian C, Xu C, Ruan J, Lee KK, Burke TL, Tempel W, Barsyte D, Li J, Wu M, Zhou BO, Fleharty BE, Paulson A, Allali-Hassani A, Zhou JQ, Mer G, Grant PA, Workman JL, Zang J, Min J EMBO J. 2011 Jun 17. doi: 10.1038/emboj.2011.193. PMID:21685874<ref>PMID:21685874</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3mp1" style="background-color:#fffaf0;"></div>
-==About this Structure==
+==See Also==
-[[3mp1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli,_undefined,_saccharomyces_cerevisiae Escherichia coli, undefined, saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MP1 OCA].
+*[[SAGA-associated factor|SAGA-associated factor]]
-[[Category: Escherichia coli, undefined, saccharomyces cerevisiae]]
+== References ==
-[[Category: Li, J.]]
+<references/>
-[[Category: Ruan, J.]]
+__TOC__
-[[Category: Wu, M.]]
+</StructureSection>
-[[Category: Xue, X.]]
+[[Category: Escherichia coli K-12]]
-[[Category: Zang, J.]]
+[[Category: Large Structures]]
+[[Category: Saccharomyces cerevisiae S288C]]
+[[Category: Synthetic construct]]
+[[Category: Unidentified]]
+[[Category: Li J]]
+[[Category: Ruan J]]
+[[Category: Wu M]]
+[[Category: Xue X]]
+[[Category: Zang J]]