1mr3

<StructureSection load='1mr3' size='340' side='right' caption='[[1mr3]], [[Resolution|resolution]] 1.60&Aring;' scene=''>

<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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MR3 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/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>

[[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.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mr/1mr3_consurf.spt"</scriptWhenChecked>

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== 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>

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== References ==

<references/>

[[Category: Atcc 18824]]

[[Category: Amor, J C]]

[[Category: Cheng, X]]

[[Category: Horton, J R]]

[[Category: Kahn, R A]]

[[Category: Ringe, D]]

[[Category: Sullards, C]]

[[Category: Wang, Y]]

[[Category: Zhu, X]]

[[Category: Small gtpase]]