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3mnm

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Crystal structure of GAE domain of GGA2p from Saccharomyces cerevisiae

Structural highlights

3mnm is a 3 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
NonStd Res:
Gene:	GGA2 (ATCC 18824)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[GGA2_YEAST] May play a role in the regulation of membrane traffic through the trans-Golgi network.^[1] ^[2]

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

Different assemblies of accessory proteins with clathrin are critical for transporting precisely various cargos between intracellular compartments. GGA proteins are adaptors for clathrin-mediated intracellular trafficking, connecting other accessory and cargo proteins to clathrin-coated vesicles. Both binding to the GAE domain of GGA protein yGGA2 in Saccharomyces cerevisia, Ent3 and Ent5 are involved in different trafficking pathways. Ent5 is ubiquitous and localized in a manner independent of yGGA2, and Ent3 functions preferentially through yGGA2. Not known are the sources of these differences. Here we show not all acidic-phenylalanine motifs in Ent3/5 are active for yGGA2_GAE domain binding. Two of the three acidic-phenylalanine motifs from Ent3 can bind to the yGGA2_GAE domain, while only one of the two motifs from Ent5 can bind. We also determined the crystal structure of the yGGA2_GAE domain at 1.8 A resolution. Structural docking and mutagenesis analysis shows inactive motifs in Ent3 and Ent5 repel yGGA2_GAE binding through disfavored residues at positions 1 and 3. These results suggest accessory proteins may fine-tune the GGA adaptor dependence by adjusting their non-acidic-phenylalanine residues, thus contributing to the distinct role of Ent3 and Ent5 in trafficking.

Structural basis for the specificity of the GAE domain of yGGA2 for its accessory proteins Ent3 and Ent5 .,Fang P, Li X, Wang J, Niu L, Teng M Biochemistry. 2010 Sep 14;49(36):7949-55. PMID:20704189^[3]

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

References

↑ Hirst J, Lui WW, Bright NA, Totty N, Seaman MN, Robinson MS. A family of proteins with gamma-adaptin and VHS domains that facilitate trafficking between the trans-Golgi network and the vacuole/lysosome. J Cell Biol. 2000 Apr 3;149(1):67-80. PMID:10747088
↑ Zhdankina O, Strand NL, Redmond JM, Boman AL. Yeast GGA proteins interact with GTP-bound Arf and facilitate transport through the Golgi. Yeast. 2001 Jan 15;18(1):1-18. PMID:11124697 doi:<1::AID-YEA644>3.0.CO;2-5 10.1002/1097-0061(200101)18:1<1::AID-YEA644>3.0.CO;2-5
↑ Fang P, Li X, Wang J, Niu L, Teng M. Structural basis for the specificity of the GAE domain of yGGA2 for its accessory proteins Ent3 and Ent5 . Biochemistry. 2010 Sep 14;49(36):7949-55. PMID:20704189 doi:http://dx.doi.org/10.1021/bi1010255

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/3mnm"

@@ Line 1: / Line 1: @@
 ==Crystal structure of GAE domain of GGA2p from Saccharomyces cerevisiae==
 <StructureSection load='3mnm' size='340' side='right' caption='[[3mnm]], [[Resolution|resolution]] 1.73&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene></td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GGA2 ([http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3mnm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mnm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mnm RCSB], [http://www.ebi.ac.uk/pdbsum/3mnm 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=3mnm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mnm OCA], [http://pdbe.org/3mnm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3mnm RCSB], [http://www.ebi.ac.uk/pdbsum/3mnm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3mnm ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mn/3mnm_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mn/3mnm_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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=3mnm ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 28: / Line 29: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3mnm" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

3mnm

From Proteopedia

Current revision

Crystal structure of GAE domain of GGA2p from Saccharomyces cerevisiae

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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