1jo8

From Proteopedia

(Difference between revisions)

Current revision

Structural analysis of the yeast actin binding protein Abp1 SH3 domain

Structural highlights

1jo8 is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.3Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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.

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Goode BL, Rodal AA, Barnes G, Drubin DG. Activation of the Arp2/3 complex by the actin filament binding protein Abp1p. J Cell Biol. 2001 Apr 30;153(3):627-34. PMID:11331312
↑ Fazi B, Cope MJ, Douangamath A, Ferracuti S, Schirwitz K, Zucconi A, Drubin DG, Wilmanns M, Cesareni G, Castagnoli L. Unusual binding properties of the SH3 domain of the yeast actin-binding protein Abp1: structural and functional analysis. J Biol Chem. 2002 Feb 15;277(7):5290-8. Epub 2001 Oct 19. PMID:11668184 doi:10.1074/jbc.M109848200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1jo8"

@@ Line 3: / Line 3: @@
 <StructureSection load='1jo8' size='340' side='right'caption='[[1jo8]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1jo8]] is a 1 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=1JO8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JO8 FirstGlance]. <br>
+<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>
-</td></tr><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>
+</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>
+<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>
 <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>
 == 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>
+[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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Atcc 18824]]
 [[Category: Large Structures]]
-[[Category: Castagnoli, L]]
+[[Category: Saccharomyces cerevisiae]]
-[[Category: Cesareni, G]]
+[[Category: Castagnoli L]]
-[[Category: Cope, M J]]
+[[Category: Cesareni G]]
-[[Category: Douangamath, A]]
+[[Category: Cope MJ]]
-[[Category: Drubin, D G]]
+[[Category: Douangamath A]]
-[[Category: Fazi, B]]
+[[Category: Drubin DG]]
-[[Category: Ferracuti, S]]
+[[Category: Fazi B]]
-[[Category: Schirwitz, K]]
+[[Category: Ferracuti S]]
-[[Category: Wilmanns, M]]
+[[Category: Schirwitz K]]
-[[Category: Zucconi, A]]
+[[Category: Wilmanns M]]
-[[Category: Sh3 domain actin-binding-protein]]
+[[Category: Zucconi A]]
-[[Category: Structural protein]]

1jo8

From Proteopedia

Current revision

Structural analysis of the yeast actin binding protein Abp1 SH3 domain

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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