3of7: Difference between revisions
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==The Crystal Structure of Prp20p from Saccharomyces cerevisiae and Its Binding Properties to Gsp1p and Histones== | ==The Crystal Structure of Prp20p from Saccharomyces cerevisiae and Its Binding Properties to Gsp1p and Histones== | ||
<StructureSection load='3of7' size='340' side='right' caption='[[3of7]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='3of7' size='340' side='right'caption='[[3of7]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3of7]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3of7]] is a 1 chain structure with sequence from [https://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=3OF7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OF7 FirstGlance]. <br> | ||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MTR1, PRP20, SRM1, YGL097W ([ | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MTR1, PRP20, SRM1, YGL097W ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3of7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3of7 OCA], [https://pdbe.org/3of7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3of7 RCSB], [https://www.ebi.ac.uk/pdbsum/3of7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3of7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/RCC1_YEAST RCC1_YEAST]] Guanine nucleotide exchange factor that promotes the exchange of GSP1/GSP2-bound GDP by GTP and controls RNA metabolism and transport. Involved in yeast pheromone response pathway and in mRNA metabolism. Involved in nuclear pore complex (NPC) assembly and required for mRNA and ribosome nuclear export. Binds chromatin and is involved NPC-mediated transcriptional control.<ref>PMID:2548085</ref> <ref>PMID:2277633</ref> <ref>PMID:1666302</ref> <ref>PMID:1865879</ref> <ref>PMID:1398069</ref> <ref>PMID:7679070</ref> <ref>PMID:8070652</ref> <ref>PMID:9971735</ref> <ref>PMID:11071906</ref> <ref>PMID:11142374</ref> <ref>PMID:11509570</ref> <ref>PMID:11589573</ref> <ref>PMID:12654904</ref> <ref>PMID:16365162</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Baker's yeast]] | [[Category: Baker's yeast]] | ||
[[Category: Large Structures]] | |||
[[Category: Ding, B]] | [[Category: Ding, B]] | ||
[[Category: Huang, H]] | [[Category: Huang, H]] |
Revision as of 13:41, 18 May 2022
The Crystal Structure of Prp20p from Saccharomyces cerevisiae and Its Binding Properties to Gsp1p and HistonesThe Crystal Structure of Prp20p from Saccharomyces cerevisiae and Its Binding Properties to Gsp1p and Histones
Structural highlights
Function[RCC1_YEAST] Guanine nucleotide exchange factor that promotes the exchange of GSP1/GSP2-bound GDP by GTP and controls RNA metabolism and transport. Involved in yeast pheromone response pathway and in mRNA metabolism. Involved in nuclear pore complex (NPC) assembly and required for mRNA and ribosome nuclear export. Binds chromatin and is involved NPC-mediated transcriptional control.[1] [2] [3] [4] [5] [6] [7] [8] [9] [10] [11] [12] [13] [14] Publication Abstract from PubMedPrp20p is the homolog of mammalian RCC1 (regulator of chromosome condensation 1) in Saccharomyces cerevisiae, which acts as the guanine nucleotide exchange factor (GEF) for Gsp1p (yeast Ran). Prp20p plays multiple roles in mRNA metabolism, nucleocytoplasmic transport and mitosis regulation. Prp20p also functions as a linker between chromatin and nuclear pore complex (NPC) which regulates the NPC-mediated boundary activity (BA). Prp20p contains an N-terminal nuclear localization signal (NLS) and a typical RCC1-like domain (RLD). Here we present the 1.9A crystal structure of the RCC1-like domain of Prp20p, which exhibits a classical seven-bladed beta-propeller. We also proved that the additional beta-wedge in Prp20p is essential for the interaction between Prp20p and Gsp1p. Based on this structure, we built a complex model of Prp20p and Gsp1p which was optimized by molecular dynamics (MD) simulations. Our model reveals that Prp20p and RCC1 share similar Ran GTPase binding mode. In addition, we also studied the histone-binding property of Prp20p in vitro. The 1.9A crystal structure of Prp20p from Saccharomyces cerevisiae and its binding properties to Gsp1p and histones.,Wu F, Liu Y, Zhu Z, Huang H, Ding B, Wu J, Shi Y J Struct Biol. 2011 Apr;174(1):213-22. Epub 2010 Nov 18. PMID:21093592[15] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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