3fma: Difference between revisions
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==Crystal structure of the GYF domain of Smy2 in complex with a proline-rich peptide from BBP/ScSF1== | ==Crystal structure of the GYF domain of Smy2 in complex with a proline-rich peptide from BBP/ScSF1== | ||
<StructureSection load='3fma' size='340' side='right' caption='[[3fma]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='3fma' size='340' side='right'caption='[[3fma]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3fma]] is a 10 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3fma]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FMA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FMA FirstGlance]. <br> | ||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1l2z|1l2z]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1l2z|1l2z]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SMY2 ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SMY2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=3fma FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fma OCA], [https://pdbe.org/3fma PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fma RCSB], [https://www.ebi.ac.uk/pdbsum/3fma PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fma ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/SMY2_YEAST SMY2_YEAST]] Suppressor of the MYO2 gene. [[https://www.uniprot.org/uniprot/BBP_YEAST BBP_YEAST]] Required for pre-spliceosome formation, which is the first step of pre-mRNA splicing. 2 commitment complexes, CC1 and CC2, have been defined. CC1 is a basal complex dependent only on the 5'-splice site. CC2 is a complex of lower mobility and is dependent on a branchpoint as well as a 5'-splice site region. This protein is involved in CC2 formation where it binds to the snRNP U1-associated protein PRP40, bridging the U1 snRNP-associated 5'-splice site and the MSL5-associated branch point 3' intron splice site. Involved in nuclear retention of pre-mRNA.<ref>PMID:9150140</ref> <ref>PMID:10376880</ref> <ref>PMID:10775271</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fm/3fma_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fm/3fma_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Atcc 18824]] | [[Category: Atcc 18824]] | ||
[[Category: Large Structures]] | |||
[[Category: Ash, M R]] | [[Category: Ash, M R]] | ||
[[Category: Faelber, K]] | [[Category: Faelber, K]] | ||
| Line 31: | Line 32: | ||
[[Category: Gyf domain]] | [[Category: Gyf domain]] | ||
[[Category: Poly-proline binding]] | [[Category: Poly-proline binding]] | ||
[[Category: Pr]] | |||
[[Category: Proline-rich peptide]] | [[Category: Proline-rich peptide]] | ||
[[Category: Protein binding]] | [[Category: Protein binding]] | ||
[[Category: Ragnya]] | [[Category: Ragnya]] | ||
Revision as of 08:04, 2 March 2022
Crystal structure of the GYF domain of Smy2 in complex with a proline-rich peptide from BBP/ScSF1
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