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| <StructureSection load='4y0v' size='340' side='right'caption='[[4y0v]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='4y0v' size='340' side='right'caption='[[4y0v]], [[Resolution|resolution]] 1.80Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[4y0v]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Enthi Enthi]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3rd1 3rd1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y0V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Y0V FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4y0v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Entamoeba_histolytica Entamoeba histolytica]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3rd1 3rd1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y0V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Y0V FirstGlance]. <br> |
- | </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></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]] 1.8Å</td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EHI_073470, EHI_137720 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5759 ENTHI])</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></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=4y0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y0v OCA], [http://pdbe.org/4y0v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4y0v RCSB], [http://www.ebi.ac.uk/pdbsum/4y0v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4y0v 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=4y0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y0v OCA], [https://pdbe.org/4y0v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y0v RCSB], [https://www.ebi.ac.uk/pdbsum/4y0v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y0v ProSAT]</span></td></tr> |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/C4LXL1_ENTH1 C4LXL1_ENTH1] GTP-binding protein involved in protein trafficking; modulates vesicle budding and uncoating within the Golgi apparatus.[RuleBase:RU369003] |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Enthi]] | + | [[Category: Entamoeba histolytica]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Structural genomic]] | |
- | [[Category: Signaling protein]] | |
- | [[Category: Ssgcid]] | |
| Structural highlights
Function
C4LXL1_ENTH1 GTP-binding protein involved in protein trafficking; modulates vesicle budding and uncoating within the Golgi apparatus.[RuleBase:RU369003]
Publication Abstract from PubMed
Entamoeba histolytica is the etiological agent of amebiasis, a diarrheal disease which causes amoebic liver abscesses and amoebic colitis. Approximately 50 million people are infected worldwide with E. histolytica. With only 10% of infected people developing symptomatic amebiasis, there are still an estimated 100 000 deaths each year. Because of the emergence of resistant strains of the parasite, it is necessary to find a treatment which would be a proper response to this challenge. ADP-ribosylation factor (ARF) is a member of the ARF family of GTP-binding proteins. These proteins are ubiquitous in eukaryotic cells; they generally associate with cell membranes and regulate vesicular traffic and intracellular signalling. The crystal structure of ARF1 from E. histolytica has been determined bound to magnesium and GDP at 1.8 A resolution. Comparison with other structures of eukaryotic ARF proteins shows a highly conserved structure and supports the interswitch toggle mechanism of communicating the conformational state to partner proteins.
Structure of an ADP-ribosylation factor, ARF1, from Entamoeba histolytica bound to Mg(2+)-GDP.,Serbzhinskiy DA, Clifton MC, Sankaran B, Staker BL, Edwards TE, Myler PJ Acta Crystallogr F Struct Biol Commun. 2015 May;71(Pt 5):594-9. doi:, 10.1107/S2053230X15004677. Epub 2015 Apr 21. PMID:25945714[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Serbzhinskiy DA, Clifton MC, Sankaran B, Staker BL, Edwards TE, Myler PJ. Structure of an ADP-ribosylation factor, ARF1, from Entamoeba histolytica bound to Mg(2+)-GDP. Acta Crystallogr F Struct Biol Commun. 2015 May;71(Pt 5):594-9. doi:, 10.1107/S2053230X15004677. Epub 2015 Apr 21. PMID:25945714 doi:http://dx.doi.org/10.1107/S2053230X15004677
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