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3fma

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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==
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<StructureSection load='3fma' size='340' side='right' caption='[[3fma]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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<StructureSection load='3fma' size='340' side='right'caption='[[3fma]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3fma]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FMA FirstGlance]. <br>
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<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>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1l2z|1l2z]]</td></tr>
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<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>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SMY2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</td></tr>
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<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>
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<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=3fma FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fma OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3fma RCSB], [http://www.ebi.ac.uk/pdbsum/3fma PDBsum]</span></td></tr>
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<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 ==
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[[http://www.uniprot.org/uniprot/SMY2_YEAST SMY2_YEAST]] Suppressor of the MYO2 gene. [[http://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>
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[[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>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fm/3fma_consurf.spt"</scriptWhenChecked>
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<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>
</jmolCheckbox>
</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3fma ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
== References ==
== References ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Saccharomyces cerevisiae]]
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[[Category: Atcc 18824]]
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[[Category: Large Structures]]
[[Category: Ash, M R]]
[[Category: Ash, M R]]
[[Category: Faelber, K]]
[[Category: Faelber, K]]
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[[Category: Gyf domain]]
[[Category: Gyf domain]]
[[Category: Poly-proline binding]]
[[Category: Poly-proline binding]]
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[[Category: Pr]]
[[Category: Proline-rich peptide]]
[[Category: Proline-rich peptide]]
[[Category: Protein binding]]
[[Category: Protein binding]]
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[[Category: Pr]]
 
[[Category: Ragnya]]
[[Category: Ragnya]]

Current revision

Crystal structure of the GYF domain of Smy2 in complex with a proline-rich peptide from BBP/ScSF1

PDB ID 3fma

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