1jo8: Difference between revisions

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[[Image:1jo8.jpg|left|200px]]


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==Structural analysis of the yeast actin binding protein Abp1 SH3 domain==
The line below this paragraph, containing "STRUCTURE_1jo8", creates the "Structure Box" on the page.
<StructureSection load='1jo8' size='340' side='right'caption='[[1jo8]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1jo8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JO8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JO8 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
{{STRUCTURE_1jo8|  PDB=1jo8  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jo8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jo8 OCA], [https://pdbe.org/1jo8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jo8 RCSB], [https://www.ebi.ac.uk/pdbsum/1jo8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jo8 ProSAT]</span></td></tr>
 
</table>
'''Structural analysis of the yeast actin binding protein Abp1 SH3 domain'''
== Function ==
 
[https://www.uniprot.org/uniprot/ABP1_YEAST ABP1_YEAST] Regulates ARP2/3 complex-mediated actin assembly. Recruits ARP2/3 complex to sides of preexisting actin filaments, which may promote nucleation or stabilization of filament branches. Binds to actin filaments, but not actin monomers. Actin binding is required for ARP2/3 complex activation. May also have a role in linking the actin cytoskeleton to endocytosis. recruits components of the endocytotic machinery to cortical actin patches, known sites of endocytosis.<ref>PMID:11331312</ref>
 
== Evolutionary Conservation ==
==Overview==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jo/1jo8_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1jo8 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Abp1p is an actin-binding protein that plays a central role in the organization of Saccharomyces cerevisiae actin cytoskeleton. By a combination of two-hybrid and phage-display approaches, we have identified six new ligands of the Abp1-SH3 domain. None of these SH3-mediated novel interactions was detected in recent all genome high throughput protein interaction projects. Here we show that the SH3-mediated association of Abp1p with the Ser/Thr kinases Prk1p and Ark1p is essential for their localization to actin cortical patches. The Abp1-SH3 domain has a rather unusual binding specificity, because its target peptides contain the tetrapentapeptide +XXXPXXPX+PXXL with positive charges flanking the polyproline core on both sides. Here we present the structure of the Abp1-SH3 domain solved at 1.3-A resolution. The peptide-binding pockets in the SH3 domain are flanked by two acidic residues that are uncommon at those positions in the SH3 domain family. We have shown by site-directed mutagenesis that one of these negatively charged side chains may be the key determinant for the preference for non-classical ligands.
Abp1p is an actin-binding protein that plays a central role in the organization of Saccharomyces cerevisiae actin cytoskeleton. By a combination of two-hybrid and phage-display approaches, we have identified six new ligands of the Abp1-SH3 domain. None of these SH3-mediated novel interactions was detected in recent all genome high throughput protein interaction projects. Here we show that the SH3-mediated association of Abp1p with the Ser/Thr kinases Prk1p and Ark1p is essential for their localization to actin cortical patches. The Abp1-SH3 domain has a rather unusual binding specificity, because its target peptides contain the tetrapentapeptide +XXXPXXPX+PXXL with positive charges flanking the polyproline core on both sides. Here we present the structure of the Abp1-SH3 domain solved at 1.3-A resolution. The peptide-binding pockets in the SH3 domain are flanked by two acidic residues that are uncommon at those positions in the SH3 domain family. We have shown by site-directed mutagenesis that one of these negatively charged side chains may be the key determinant for the preference for non-classical ligands.


==About this Structure==
Unusual binding properties of the SH3 domain of the yeast actin-binding protein Abp1: structural and functional analysis.,Fazi B, Cope MJ, Douangamath A, Ferracuti S, Schirwitz K, Zucconi A, Drubin DG, Wilmanns M, Cesareni G, Castagnoli L J Biol Chem. 2002 Feb 15;277(7):5290-8. Epub 2001 Oct 19. PMID:11668184<ref>PMID:11668184</ref>
1JO8 is a [[Single protein]] structure of 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=1JO8 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Unusual binding properties of the SH3 domain of the yeast actin-binding protein Abp1: structural and functional analysis., Fazi B, Cope MJ, Douangamath A, Ferracuti S, Schirwitz K, Zucconi A, Drubin DG, Wilmanns M, Cesareni G, Castagnoli L, J Biol Chem. 2002 Feb 15;277(7):5290-8. Epub 2001 Oct 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11668184 11668184]
</div>
<div class="pdbe-citations 1jo8" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Castagnoli L]]
[[Category: Castagnoli, L.]]
[[Category: Cesareni G]]
[[Category: Cesareni, G.]]
[[Category: Cope MJ]]
[[Category: Cope, M J.]]
[[Category: Douangamath A]]
[[Category: Douangamath, A.]]
[[Category: Drubin DG]]
[[Category: Drubin, D G.]]
[[Category: Fazi B]]
[[Category: Fazi, B.]]
[[Category: Ferracuti S]]
[[Category: Ferracuti, S.]]
[[Category: Schirwitz K]]
[[Category: Schirwitz, K.]]
[[Category: Wilmanns M]]
[[Category: Wilmanns, M.]]
[[Category: Zucconi A]]
[[Category: Zucconi, A.]]
[[Category: Sh3 domain actin-binding-protein]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 21:29:48 2008''
Retrieved from "https://proteopedia.org/1jo8"