1mr3: Difference between revisions

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<StructureSection load='1mr3' size='340' side='right'caption='[[1mr3]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
<StructureSection load='1mr3' size='340' side='right'caption='[[1mr3]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1mr3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MR3 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1MR3 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1mr3]] 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=1MR3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MR3 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=EOH:ETHANOL'>EOH</scene>, <scene name='pdbligand=G3D:GUANOSINE-3-MONOPHOSPHATE-5-DIPHOSPHATE'>G3D</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PDO:1,3-PROPANDIOL'>PDO</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]] 1.6&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1hur|1hur]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=EOH:ETHANOL'>EOH</scene>, <scene name='pdbligand=G3D:GUANOSINE-3-MONOPHOSPHATE-5-DIPHOSPHATE'>G3D</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PDO:1,3-PROPANDIOL'>PDO</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ARF2 ([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'>[https://proteopedia.org/fgij/fg.htm?mol=1mr3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mr3 OCA], [https://pdbe.org/1mr3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mr3 RCSB], [https://www.ebi.ac.uk/pdbsum/1mr3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mr3 ProSAT]</span></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=1mr3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mr3 OCA], [http://pdbe.org/1mr3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mr3 RCSB], [http://www.ebi.ac.uk/pdbsum/1mr3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mr3 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/ARF2_YEAST ARF2_YEAST]] GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus.  
[https://www.uniprot.org/uniprot/ARF2_YEAST ARF2_YEAST] GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1mr3 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=1mr3 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Structures were determined by x-ray crystallography for two members of the ADP-ribosylation factor (ARF) family of regulatory GTPases, yeast ARF1 and ARL1, and were compared with previously determined structures of human ARF1 and ARF6. These analyses revealed an overall conserved fold but differences in primary sequence and length, particularly in an N-terminal loop, lead to differences in nucleotide and divalent metal binding. Packing of hydrophobic residues is central to the interplay between the N-terminal alpha-helix, switch I, and the interswitch region, which along with differences in surface electrostatics provide explanations for the different biophysical and biochemical properties of ARF and ARF-like proteins.
Structures of yeast ARF2 and ARL1: distinct roles for the N terminus in the structure and function of ARF family GTPases.,Amor JC, Horton JR, Zhu X, Wang Y, Sullards C, Ringe D, Cheng X, Kahn RA J Biol Chem. 2001 Nov 9;276(45):42477-84. Epub 2001 Sep 4. PMID:11535602<ref>PMID:11535602</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1mr3" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 18824]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Amor, J C]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Cheng, X]]
[[Category: Amor J-C]]
[[Category: Horton, J R]]
[[Category: Cheng X]]
[[Category: Kahn, R A]]
[[Category: Horton JR]]
[[Category: Ringe, D]]
[[Category: Kahn RA]]
[[Category: Sullards, C]]
[[Category: Ringe D]]
[[Category: Wang, Y]]
[[Category: Sullards C]]
[[Category: Zhu, X]]
[[Category: Wang Y]]
[[Category: Gdp-3'phosphate]]
[[Category: Zhu X]]
[[Category: Gtp-binding]]
[[Category: Signal transduction]]
[[Category: Signaling protein]]
[[Category: Small gtpase]]

Latest revision as of 10:47, 14 February 2024

Saccharomyces cerevisiae ADP-ribosylation Factor 2 (ScArf2) complexed with GDP-3'P at 1.6A resolutionSaccharomyces cerevisiae ADP-ribosylation Factor 2 (ScArf2) complexed with GDP-3'P at 1.6A resolution

Structural highlights

1mr3 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 1.6Å
Ligands:, , , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ARF2_YEAST GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus.

Evolutionary Conservation

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

1mr3, resolution 1.60Å

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OCA
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