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1om9

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Revision as of 08:00, 15 February 2018

Structure of the GGA1-appendage in complex with the p56 binding peptide

Structural highlights

1om9 is a 4 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1na8, 1gyu, 1iu1
Gene:	GGA1 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[GGA1_HUMAN] Plays a role in protein sorting and trafficking between the trans-Golgi network (TGN) and endosomes. Mediates the ARF-dependent recruitment of clathrin to the TGN and binds ubiquitinated proteins and membrane cargo molecules with a cytosolic acidic cluster-dileucine (AC-LL) motif.^[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

The Golgi-associated, gamma-adaptin-related, ADP-ribosylation-factor binding proteins (GGAs) and adaptor protein (AP)-1 are adaptors involved in clathrin-mediated transport between the trans-Golgi network and endosomal system. The appendage domains of GGAs and the AP-1 gamma-adaptin subunit are structurally homologous and have been proposed to bind to accessory proteins via interaction with short sequences containing phenylalanines and acidic residues. Here we present the structure of the human GGA1 appendage in complex with its cognate binding peptide from the p56 accessory protein (DDDDFGGFEAAETFD) as determined by X-ray crystallography. The interaction is governed predominantly by packing of the first two phenylalanine residues of the peptide with conserved basic and hydrophobic residues from GGA1. Additionally, several main chain hydrogen bonds cause the peptide to form an additional beta-strand on the edge of the preexisting beta-sheet of the protein. Isothermal titration calorimetry was used to assess the affinities of different peptides for the GGA and gamma-appendage domains.

Structural basis for binding of accessory proteins by the appendage domain of GGAs.,Collins BM, Praefcke GJ, Robinson MS, Owen DJ Nat Struct Biol. 2003 Aug;10(8):607-13. PMID:12858163^[2]

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

References

↑ Puertollano R, Randazzo PA, Presley JF, Hartnell LM, Bonifacino JS. The GGAs promote ARF-dependent recruitment of clathrin to the TGN. Cell. 2001 Apr 6;105(1):93-102. PMID:11301005
↑ Collins BM, Praefcke GJ, Robinson MS, Owen DJ. Structural basis for binding of accessory proteins by the appendage domain of GGAs. Nat Struct Biol. 2003 Aug;10(8):607-13. PMID:12858163 doi:10.1038/nsb955

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/1om9"

@@ Line 1: / Line 1: @@
 ==Structure of the GGA1-appendage in complex with the p56 binding peptide==
 <StructureSection load='1om9' size='340' side='right' caption='[[1om9]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1na8|1na8]], [[1gyu|1gyu]], [[1iu1|1iu1]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GGA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-<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=1om9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1om9 OCA], [http://pdbe.org/1om9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1om9 RCSB], [http://www.ebi.ac.uk/pdbsum/1om9 PDBsum]</span></td></tr>
+<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=1om9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1om9 OCA], [http://pdbe.org/1om9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1om9 RCSB], [http://www.ebi.ac.uk/pdbsum/1om9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1om9 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/om/1om9_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/om/1om9_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

1om9

From Proteopedia

Revision as of 08:00, 15 February 2018

Structure of the GGA1-appendage in complex with the p56 binding peptide

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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