1ow3: Difference between revisions

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<StructureSection load='1ow3' size='340' side='right'caption='[[1ow3]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='1ow3' size='340' side='right'caption='[[1ow3]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1ow3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OW3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OW3 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1ow3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OW3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OW3 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=MGF:TRIFLUOROMAGNESATE'>MGF</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]] 1.8&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RHOGAP1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), RHOA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=MGF:TRIFLUOROMAGNESATE'>MGF</scene></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=1ow3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ow3 OCA], [https://pdbe.org/1ow3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ow3 RCSB], [https://www.ebi.ac.uk/pdbsum/1ow3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ow3 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=1ow3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ow3 OCA], [https://pdbe.org/1ow3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ow3 RCSB], [https://www.ebi.ac.uk/pdbsum/1ow3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ow3 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/RHG01_HUMAN RHG01_HUMAN]] GTPase activator for the Rho, Rac and Cdc42 proteins, converting them to the putatively inactive GDP-bound state. Cdc42 seems to be the preferred substrate. [[https://www.uniprot.org/uniprot/RHOA_HUMAN RHOA_HUMAN]] Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Involved in a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Plays an essential role in cleavage furrow formation. Required for the apical junction formation of keratinocyte cell-cell adhesion. Serves as a target for the yopT cysteine peptidase from Yersinia pestis, vector of the plague, and Yersinia pseudotuberculosis, which causes gastrointestinal disorders. Stimulates PKN2 kinase activity. May be an activator of PLCE1. Activated by ARHGEF2, which promotes the exchange of GDP for GTP. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization.<ref>PMID:8910519</ref> <ref>PMID:9121475</ref> <ref>PMID:12900402</ref> <ref>PMID:16103226</ref> <ref>PMID:16236794</ref> <ref>PMID:19934221</ref> <ref>PMID:20937854</ref> <ref>PMID:20974804</ref> 
[https://www.uniprot.org/uniprot/RHG01_HUMAN RHG01_HUMAN] GTPase activator for the Rho, Rac and Cdc42 proteins, converting them to the putatively inactive GDP-bound state. Cdc42 seems to be the preferred substrate.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Eccleston, J F]]
[[Category: Eccleston JF]]
[[Category: Gamblin, S J]]
[[Category: Gamblin SJ]]
[[Category: Graham, D L]]
[[Category: Graham DL]]
[[Category: Grime, G W]]
[[Category: Grime GW]]
[[Category: Lowe, P N]]
[[Category: Lowe PN]]
[[Category: Marsh, M]]
[[Category: Marsh M]]
[[Category: Rittinger, K]]
[[Category: Rittinger K]]
[[Category: Smerdon, S J]]
[[Category: Smerdon SJ]]
[[Category: Complex]]
[[Category: Gap]]
[[Category: Gene regulation-signaling protein complex]]
[[Category: Gtpase]]
[[Category: Transition state]]

Latest revision as of 12:33, 16 August 2023

Crystal Structure of RhoA.GDP.MgF3-in Complex with RhoGAPCrystal Structure of RhoA.GDP.MgF3-in Complex with RhoGAP

Structural highlights

1ow3 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RHG01_HUMAN GTPase activator for the Rho, Rac and Cdc42 proteins, converting them to the putatively inactive GDP-bound state. Cdc42 seems to be the preferred substrate.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The formation of complexes between small G proteins and certain of their effectors can be facilitated by aluminum fluorides. Solution studies suggest that magnesium may be able to replace aluminum in such complexes. We have determined the crystal structure of RhoA.GDP bound to RhoGAP in the presence of Mg(2+) and F(-) but without Al(3+). The metallofluoride adopts a trigonal planar arrangement instead of the square planar structure of AlF(4)(-). We have confirmed that these crystals contain magnesium and not aluminum by proton-induced X-ray emission spectroscopy. The structure adopted by GDP.MgF(-) possesses the stereochemistry and approximate charge expected for the transition state. We suggest that MgF3(-) may be the reagent of choice for studying phosphoryl transfer reactions.

MgF(3)(-) as a transition state analog of phosphoryl transfer.,Graham DL, Lowe PN, Grime GW, Marsh M, Rittinger K, Smerdon SJ, Gamblin SJ, Eccleston JF Chem Biol. 2002 Mar;9(3):375-81. PMID:11927263[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Graham DL, Lowe PN, Grime GW, Marsh M, Rittinger K, Smerdon SJ, Gamblin SJ, Eccleston JF. MgF(3)(-) as a transition state analog of phosphoryl transfer. Chem Biol. 2002 Mar;9(3):375-81. PMID:11927263

1ow3, resolution 1.80Å

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