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6a8d

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Current revision (09:21, 22 November 2023) (edit) (undo)
 
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<StructureSection load='6a8d' size='340' side='right'caption='[[6a8d]], [[Resolution|resolution]] 2.34&Aring;' scene=''>
<StructureSection load='6a8d' size='340' side='right'caption='[[6a8d]], [[Resolution|resolution]] 2.34&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6a8d]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A8D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6A8D FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6a8d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A8D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6A8D FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.34&#8491;</td></tr>
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<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=6a8d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a8d OCA], [http://pdbe.org/6a8d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6a8d RCSB], [http://www.ebi.ac.uk/pdbsum/6a8d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6a8d ProSAT]</span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6a8d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a8d OCA], [https://pdbe.org/6a8d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6a8d RCSB], [https://www.ebi.ac.uk/pdbsum/6a8d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6a8d ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A8ILA3_CHLRE A8ILA3_CHLRE]
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GTPases of the Ras superfamily regulate a wide variety of cellular processes including vesicular transport and various secretory pathways of the cell. ADP - ribosylation factor (ARF) belongs to one of the five major families of the Ras superfamily and serves as an important component of vesicle formation and transport machinery of the cells. The binding of GTP to these Arfs and its subsequent hydrolysis, induces conformational changes in these proteins leading to their enzymatic activities. The dimeric form of Arf is associated with membrane pinch-off during vesicle formation. In this report, we have identified an arf gene from the unicellular green alga Chlamydomonas reinhardtii, CrArf, and showed that the oligomeric state of the protein in C. renhardtii is modulated by the cellular membrane environment of the organism. Protein cross-linking experiments showed that the purified recombinant CrArf has the ability to form a dimer. Both the 20-kDa monomeric and 40-kDa dimeric forms of CrArf were recognized from Chlamydomonas total cell lysate (CrTLC) and purified recombinant CrArf by the CrArf specific antibody. The membranous environment of the cell appeared to facilitate dimerization of the CrArf, as dimeric form was found exclusively associated with the membrane bound organelles. The subcellular localization studies in Chlamydomonas suggested that CrArf mainly localized in the cytosol and was mislocalized in vesicle transport machinery inhibitor treated cells. This research sheds light on the importance of the cellular membrane environment for regulating the oligomeric state of CrArf protein in this organism and associated functional role.
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Cellular organelles facilitate dimerization of a newly identified Arf from Chlamydomonas reinhardtii.,Ranjan P, Kashyap RS, Goel M, Veetil SK, Kateriya S J Phycol. 2014 Dec;50(6):1137-45. doi: 10.1111/jpy.12245. Epub 2014 Nov 10. PMID:26988793<ref>PMID:26988793</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6a8d" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Large Structures]]
 
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[[Category: Goel, M]]
 
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[[Category: Kateriya, S]]
 
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[[Category: Kumari, S]]
 
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[[Category: Sharma, P]]
 
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[[Category: Adp-ribosylation factor]]
 
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[[Category: Arf]]
 
[[Category: Chlamydomonas reinhardtii]]
[[Category: Chlamydomonas reinhardtii]]
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[[Category: Protein transport]]
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[[Category: Large Structures]]
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[[Category: Goel M]]
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[[Category: Kateriya S]]
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[[Category: Kumari S]]
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[[Category: Sharma P]]

Current revision

Crystal Structure of Chlamydomonas reinhardtii ARF

PDB ID 6a8d

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