5ee5

From Proteopedia

(Difference between revisions)

Revision as of 06:55, 22 April 2020

Structure of human ARL1 in complex with the DCB domain of BIG1

Structural highlights

5ee5 is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , , ,
NonStd Res:
Related:	4dcn, 1upt
Gene:	ARFGEF1, ARFGEP1, BIG1 (HUMAN), ARL1 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[BIG1_HUMAN] Promotes guanine-nucleotide exchange on ARF1 and ARF3. Promotes the activation of ARF1/ARF3 through replacement of GDP with GTP. Involved in vesicular trafficking. Required for the maintenance of Golgi structure; the function may be independent of its GEF activity. Required for the maturaion of integrin beta-1 in the Golgi. Involved in the establishment and persistence of cell polarity during directed cell movement in wound healing. Proposed to act as A kinase-anchoring protein (AKAP) and may mediate crosstalk between Arf and PKA pathways. Inhibits GAP activity of MYO9B probably through competetive RhoA binding. The function in the nucleus remains to be determined.^[1] ^[2] ^[3] ^[4] ^[5] [ARL1_HUMAN] GTP-binding protein that has very low efficiency as allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. Can activate phospholipase D with very low efficiency. Important for normal function of the Golgi apparatus.^[6]

Publication Abstract from PubMed

The GTPase Arf1 is the major regulator of vesicle traffic at both the cis- and trans-Golgi. Arf1 is activated at the cis-Golgi by the guanine nucleotide exchange factor (GEF) GBF1 and at the trans-Golgi by the related GEF BIG1 or its paralog, BIG2. The trans-Golgi-specific targeting of BIG1 and BIG2 depends on the Arf-like GTPase Arl1. We find that Arl1 binds to the dimerization and cyclophilin binding (DCB) domain in BIG1 and report a crystal structure of human Arl1 bound to this domain. Residues in the DCB domain that bind Arl1 are required for BIG1 to locate to the Golgi in vivo. DCB domain-binding residues in Arl1 have a distinct conformation from those in known Arl1-effector complexes, and this plasticity allows Arl1 to interact with different effectors of unrelated structure. The findings provide structural insight into how Arf1 GEFs, and hence active Arf1, achieve their correct subcellular distribution.

Structural Insights into Arl1-Mediated Targeting of the Arf-GEF BIG1 to the trans-Golgi.,Galindo A, Soler N, McLaughlin SH, Yu M, Williams RL, Munro S Cell Rep. 2016 Jun 29. pii: S2211-1247(16)30762-8. doi:, 10.1016/j.celrep.2016.06.022. PMID:27373159^[7]

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

References

↑ Li H, Adamik R, Pacheco-Rodriguez G, Moss J, Vaughan M. Protein kinase A-anchoring (AKAP) domains in brefeldin A-inhibited guanine nucleotide-exchange protein 2 (BIG2). Proc Natl Acad Sci U S A. 2003 Feb 18;100(4):1627-32. Epub 2003 Feb 5. PMID:12571360 doi:10.1073/pnas.0337678100
↑ Saeki N, Tokuo H, Ikebe M. BIG1 is a binding partner of myosin IXb and regulates its Rho-GTPase activating protein activity. J Biol Chem. 2005 Mar 18;280(11):10128-34. Epub 2005 Jan 11. PMID:15644318 doi:10.1074/jbc.M413415200
↑ Shen X, Hong MS, Moss J, Vaughan M. BIG1, a brefeldin A-inhibited guanine nucleotide-exchange protein, is required for correct glycosylation and function of integrin beta1. Proc Natl Acad Sci U S A. 2007 Jan 23;104(4):1230-5. Epub 2007 Jan 16. PMID:17227842 doi:10.1073/pnas.0610535104
↑ Li CC, Kuo JC, Waterman CM, Kiyama R, Moss J, Vaughan M. Effects of brefeldin A-inhibited guanine nucleotide-exchange (BIG) 1 and KANK1 proteins on cell polarity and directed migration during wound healing. Proc Natl Acad Sci U S A. 2011 Nov 29;108(48):19228-33. doi:, 10.1073/pnas.1117011108. Epub 2011 Nov 14. PMID:22084092 doi:10.1073/pnas.1117011108
↑ Boal F, Stephens DJ. Specific functions of BIG1 and BIG2 in endomembrane organization. PLoS One. 2010 Mar 25;5(3):e9898. doi: 10.1371/journal.pone.0009898. PMID:20360857 doi:10.1371/journal.pone.0009898
↑ Hong JX, Lee FJ, Patton WA, Lin CY, Moss J, Vaughan M. Phospholipid- and GTP-dependent activation of cholera toxin and phospholipase D by human ADP-ribosylation factor-like protein 1 (HARL1). J Biol Chem. 1998 Jun 19;273(25):15872-6. PMID:9624189
↑ Galindo A, Soler N, McLaughlin SH, Yu M, Williams RL, Munro S. Structural Insights into Arl1-Mediated Targeting of the Arf-GEF BIG1 to the trans-Golgi. Cell Rep. 2016 Jun 29. pii: S2211-1247(16)30762-8. doi:, 10.1016/j.celrep.2016.06.022. PMID:27373159 doi:http://dx.doi.org/10.1016/j.celrep.2016.06.022

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5ee5"

@@ Line 1: / Line 1: @@
 ==Structure of human ARL1 in complex with the DCB domain of BIG1==
-<StructureSection load='5ee5' size='340' side='right' caption='[[5ee5]], [[Resolution|resolution]] 2.28&Aring;' scene=''>
+<StructureSection load='5ee5' size='340' side='right'caption='[[5ee5]], [[Resolution|resolution]] 2.28&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5ee5]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EE5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EE5 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5ee5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EE5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5EE5 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4dcn|4dcn]], [[1upt|1upt]]</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=5ee5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ee5 OCA], [http://pdbe.org/5ee5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ee5 RCSB], [http://www.ebi.ac.uk/pdbsum/5ee5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ee5 ProSAT]</span></td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ARFGEF1, ARFGEP1, BIG1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), ARL1 ([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://proteopedia.org/fgij/fg.htm?mol=5ee5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ee5 OCA], [http://pdbe.org/5ee5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ee5 RCSB], [http://www.ebi.ac.uk/pdbsum/5ee5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ee5 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 24: / Line 25: @@
 __TOC__
 </StructureSection>
+[[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Galindo, A]]
 [[Category: Munro, S]]

5ee5

From Proteopedia

Revision as of 06:55, 22 April 2020

Structure of human ARL1 in complex with the DCB domain of BIG1

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox