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| <StructureSection load='3lrp' size='340' side='right'caption='[[3lrp]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='3lrp' size='340' side='right'caption='[[3lrp]], [[Resolution|resolution]] 2.50Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[3lrp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Plafa Plafa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LRP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LRP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3lrp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LRP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LRP FirstGlance]. <br> |
- | </td></tr><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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3lro|3lro]]</div></td></tr> | + | <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> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ARF1, ARF, PLARF ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5833 PLAFA])</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=3lrp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lrp OCA], [https://pdbe.org/3lrp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lrp RCSB], [https://www.ebi.ac.uk/pdbsum/3lrp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lrp ProSAT]</span></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=3lrp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lrp OCA], [https://pdbe.org/3lrp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lrp RCSB], [https://www.ebi.ac.uk/pdbsum/3lrp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lrp ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[https://www.uniprot.org/uniprot/ARF1_PLAFA ARF1_PLAFA]] GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus (By similarity).
| + | [https://www.uniprot.org/uniprot/ARF1_PLAF7 ARF1_PLAF7] Small GTPase involved in protein trafficking between different compartments (PubMed:21045287). Modulates vesicle budding and uncoating within the Golgi complex (By similarity). In its GTP-bound form, triggers the recruitment of coatomer proteins to the Golgi membrane (By similarity). The hydrolysis of ARF1-bound GTP, which is mediated by ARFGAPs proteins, is required for dissociation of coat proteins from Golgi membranes and vesicles (By similarity). Regulates the transport of N-acylated AK2 to the parasitophorous vacuole membrane (PubMed:33604307). May be involved in the activation of lipid kinase PIP5K (PubMed:19171150).[UniProtKB:P84077]<ref>PMID:19171150</ref> <ref>PMID:21045287</ref> <ref>PMID:33604307</ref> |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| </StructureSection> | | </StructureSection> |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Plafa]] | + | [[Category: Plasmodium falciparum]] |
- | [[Category: Chattopadhyay, D]] | + | [[Category: Chattopadhyay D]] |
- | [[Category: Cook, W J]] | + | [[Category: Cook WJ]] |
- | [[Category: Adp-ribosylation factor]]
| + | |
- | [[Category: Er-golgi transport]]
| + | |
- | [[Category: Golgi apparatus]]
| + | |
- | [[Category: Gtp-binding]]
| + | |
- | [[Category: Lipoprotein]]
| + | |
- | [[Category: Myristate]]
| + | |
- | [[Category: Nucleotide-binding]]
| + | |
- | [[Category: Protein trafficking]]
| + | |
- | [[Category: Protein transport]]
| + | |
- | [[Category: Signaling protein]]
| + | |
- | [[Category: Transport]]
| + | |
| Structural highlights
Function
ARF1_PLAF7 Small GTPase involved in protein trafficking between different compartments (PubMed:21045287). Modulates vesicle budding and uncoating within the Golgi complex (By similarity). In its GTP-bound form, triggers the recruitment of coatomer proteins to the Golgi membrane (By similarity). The hydrolysis of ARF1-bound GTP, which is mediated by ARFGAPs proteins, is required for dissociation of coat proteins from Golgi membranes and vesicles (By similarity). Regulates the transport of N-acylated AK2 to the parasitophorous vacuole membrane (PubMed:33604307). May be involved in the activation of lipid kinase PIP5K (PubMed:19171150).[UniProtKB:P84077][1] [2] [3]
Publication Abstract from PubMed
Vesicular trafficking may play a crucial role in the pathogenesis and survival of the malaria parasite. ADP-ribosylation factors (ARFs) are among the major components of vesicular trafficking pathways in eukaryotes. The crystal structure of ARF1 GTPase from Plasmodium falciparum has been determined in the GDP-bound conformation at 2.5 A resolution and is compared with the structures of mammalian ARF1s.
Structure of Plasmodium falciparum ADP-ribosylation factor 1.,Cook WJ, Smith CD, Senkovich O, Holder AA, Chattopadhyay D Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Nov 1;66(Pt, 11):1426-31. Epub 2010 Oct 27. PMID:21045287[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Leber W, Skippen A, Fivelman QL, Bowyer PW, Cockcroft S, Baker DA. A unique phosphatidylinositol 4-phosphate 5-kinase is activated by ADP-ribosylation factor in Plasmodium falciparum. Int J Parasitol. 2009 May;39(6):645-53. PMID:19171150 doi:10.1016/j.ijpara.2008.11.015
- ↑ Cook WJ, Smith CD, Senkovich O, Holder AA, Chattopadhyay D. Structure of Plasmodium falciparum ADP-ribosylation factor 1. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Nov 1;66(Pt, 11):1426-31. Epub 2010 Oct 27. PMID:21045287 doi:10.1107/S1744309110036997
- ↑ Taku I, Hirai T, Makiuchi T, Shinzawa N, Iwanaga S, Annoura T, Nagamune K, Nozaki T, Saito-Nakano Y. Rab5b-Associated Arf1 GTPase Regulates Export of N-Myristoylated Adenylate Kinase 2 From the Endoplasmic Reticulum in Plasmodium falciparum. Front Cell Infect Microbiol. 2021 Feb 2;10:610200. PMID:33604307 doi:10.3389/fcimb.2020.610200
- ↑ Cook WJ, Smith CD, Senkovich O, Holder AA, Chattopadhyay D. Structure of Plasmodium falciparum ADP-ribosylation factor 1. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Nov 1;66(Pt, 11):1426-31. Epub 2010 Oct 27. PMID:21045287 doi:10.1107/S1744309110036997
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