3mp6: Difference between revisions
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<StructureSection load='3mp6' size='340' side='right'caption='[[3mp6]], [[Resolution|resolution]] 1.48Å' scene=''> | <StructureSection load='3mp6' size='340' side='right'caption='[[3mp6]], [[Resolution|resolution]] 1.48Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3mp6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3mp6]] 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=3MP6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MP6 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.48Å</td></tr> | ||
<tr id=' | <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=MLY:N-DIMETHYL-LYSINE'>MLY</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=3mp6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mp6 OCA], [https://pdbe.org/3mp6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mp6 RCSB], [https://www.ebi.ac.uk/pdbsum/3mp6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mp6 ProSAT]</span></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=3mp6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mp6 OCA], [https://pdbe.org/3mp6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mp6 RCSB], [https://www.ebi.ac.uk/pdbsum/3mp6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mp6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == 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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli K-12]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Saccharomyces cerevisiae S288C]] | ||
[[Category: | [[Category: Synthetic construct]] | ||
[[Category: | [[Category: Unidentified]] | ||
[[Category: | [[Category: Li J]] | ||
[[Category: | [[Category: Ruan J]] | ||
[[Category: | [[Category: Wu M]] | ||
[[Category: | [[Category: Zang J]] | ||