3lvq
From Proteopedia
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- | + | ==The crystal structure of ASAP3 in complex with Arf6 in transition state== | |
- | === | + | <StructureSection load='3lvq' size='340' side='right' caption='[[3lvq]], [[Resolution|resolution]] 3.38Å' scene=''> |
- | + | == Structural highlights == | |
+ | <table><tr><td colspan='2'>[[3lvq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LVQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LVQ FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AF3:ALUMINUM+FLUORIDE'>AF3</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
+ | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3lvr|3lvr]]</td></tr> | ||
+ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ASAP3, ARF6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3lvq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lvq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lvq RCSB], [http://www.ebi.ac.uk/pdbsum/3lvq PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lv/3lvq_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Arfs are small G proteins that have a key role in vesicle trafficking and cytoskeletal remodeling. ArfGAP proteins stimulate Arf intrinsic GTP hydrolysis by a mechanism that is still unresolved. Using a fusion construct we solved the structure of the ArfGAP ASAP3 in complex with Arf6 in the transition state. This structure clarifies the ArfGAP catalytic mechanism and shows a glutamine((Arf6)) and an arginine finger((ASAP3)) as the important catalytic residues. Unexpectedly the structure shows a calcium ion, liganded by both proteins in the complex interface, stabilizing the interaction and orienting the catalytic machinery. Calcium stimulates the GAP activity of ASAPs, but not other members of the ArfGAP family. This type of regulation is unique for GAPs and any other calcium-regulated processes and hints at a crosstalk between Ca(2+) and Arf signaling. | ||
- | + | The structure of an Arf-ArfGAP complex reveals a Ca2+ regulatory mechanism.,Ismail SA, Vetter IR, Sot B, Wittinghofer A Cell. 2010 May 28;141(5):812-21. PMID:20510928<ref>PMID:20510928</ref> | |
- | + | ||
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
- | == | + | <references/> |
- | + | __TOC__ | |
+ | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
- | [[Category: Ismail, S A | + | [[Category: Ismail, S A]] |
- | [[Category: Sot, B | + | [[Category: Sot, B]] |
- | [[Category: Vetter, I R | + | [[Category: Vetter, I R]] |
- | [[Category: Wittinghofer, A | + | [[Category: Wittinghofer, A]] |
[[Category: Ank repeat]] | [[Category: Ank repeat]] | ||
[[Category: Arf]] | [[Category: Arf]] |
Revision as of 15:07, 18 December 2014
The crystal structure of ASAP3 in complex with Arf6 in transition state
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Categories: Homo sapiens | Ismail, S A | Sot, B | Vetter, I R | Wittinghofer, A | Ank repeat | Arf | Arf6 | Arfgap | Asap3 | Cell membrane | Endosome | Er-golgi transport | Gap | Gdp | Golgi apparatus | Gtp-binding | Linker | Lipoprotein | Metal-binding | Myristate | Nucleotide-binding | Phosphoprotein | Protein transport | Transport | Uplc1 | Zinc-finger