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| | <StructureSection load='5u4u' size='340' side='right'caption='[[5u4u]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='5u4u' size='340' side='right'caption='[[5u4u]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5u4u]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/African_clawed_frog African clawed frog]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5U4U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5U4U FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5u4u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5U4U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5U4U FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 1.9Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5u4v|5u4v]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">arhgap35, MGC81300 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 African clawed frog])</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=5u4u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5u4u OCA], [https://pdbe.org/5u4u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5u4u RCSB], [https://www.ebi.ac.uk/pdbsum/5u4u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5u4u ProSAT]</span></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=5u4u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5u4u OCA], [http://pdbe.org/5u4u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5u4u RCSB], [http://www.ebi.ac.uk/pdbsum/5u4u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5u4u ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A1L8F832_XENLA A0A1L8F832_XENLA] |
| | <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: African clawed frog]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Boggon, T J]] | + | [[Category: Xenopus laevis]] |
| - | [[Category: Stiegler, A L]] | + | [[Category: Boggon TJ]] |
| - | [[Category: Arhgap35]] | + | [[Category: Stiegler AL]] |
| - | [[Category: Arhgap5]]
| + | |
| - | [[Category: G domain]]
| + | |
| - | [[Category: Gap]]
| + | |
| - | [[Category: Gtpase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Pseudogtpase]]
| + | |
| - | [[Category: Rho]]
| + | |
| Structural highlights
Function
A0A1L8F832_XENLA
Publication Abstract from PubMed
The two p190RhoGAP proteins, p190RhoGAP-A and -B, are key regulators of Rho GTPase signaling and are essential for actin cytoskeletal structure and contractility. Here we report the discovery of two evolutionarily conserved GTPase-like domains located in the 'middle domain', previously thought to be unstructured. Deletion of these domains reduces RhoGAP activity. Crystal structures, MANT-GTPgammaS binding, thermal denaturation, biochemical assays and sequence homology analysis all strongly support defects in nucleotide-binding activity. Analysis of p190RhoGAP proteins therefore indicates the presence of two previously unidentified domains which represent an emerging group of pseudoenzymes, the pseudoGTPases.A growing number of 'pseudoenzymes' with a regulatory role in signal transduction processes but without catalytic activity are being identified. Here, the authors identify two pseudoGTPase domains in p190RhoGAP, characterize them biochemically and structurally and show that they influence RhoGAP activity.
p190RhoGAP proteins contain pseudoGTPase domains.,Stiegler AL, Boggon TJ Nat Commun. 2017 Sep 11;8(1):506. doi: 10.1038/s41467-017-00483-x. PMID:28894085[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Stiegler AL, Boggon TJ. p190RhoGAP proteins contain pseudoGTPase domains. Nat Commun. 2017 Sep 11;8(1):506. doi: 10.1038/s41467-017-00483-x. PMID:28894085 doi:http://dx.doi.org/10.1038/s41467-017-00483-x
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