1kmt

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[[Image:1kmt.gif|left|200px]]
 
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==Crystal structure of RhoGDI Glu(154,155)Ala mutant==
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The line below this paragraph, containing "STRUCTURE_1kmt", creates the "Structure Box" on the page.
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<StructureSection load='1kmt' size='340' side='right'caption='[[1kmt]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1kmt]] 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=1KMT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KMT FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kmt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kmt OCA], [https://pdbe.org/1kmt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kmt RCSB], [https://www.ebi.ac.uk/pdbsum/1kmt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kmt ProSAT]</span></td></tr>
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{{STRUCTURE_1kmt| PDB=1kmt | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GDIR1_HUMAN GDIR1_HUMAN] Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. In glioma cells, inhibits cell migration and invasion by mediating the signals of SEMA5A and PLXNB3 that lead to inactivation of RAC1 (By similarity).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/km/1kmt_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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/main_output.php?pdb_ID=1kmt ConSurf].
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<div style="clear:both"></div>
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'''Crystal structure of RhoGDI Glu(154,155)Ala mutant'''
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==See Also==
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*[[Guanine nucleotide dissociation inhibitor|Guanine nucleotide dissociation inhibitor]]
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__TOC__
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==Overview==
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</StructureSection>
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It is hypothesized that surface residues with high conformational entropy, specifically lysines and glutamates, impede protein crystallization. In a previous study using a model system of Rho-specific guanine nucleotide dissociation inhibitor (RhoGDI), it was shown that mutating Lys residues to Ala results in enhanced crystallizability, particularly when clusters of lysines are targeted. It was also shown that one of these mutants formed crystals that yielded diffraction to 2.0 A, a significant improvement on the wild-type protein crystals. In the current paper, an analysis of the impact of surface mutations replacing Glu residues with Ala or Asp on the stability and crystallization properties of RhoGDI is presented. The Glu--&gt;Ala (Asp) mutants are generally more likely to produce crystals of the protein than the wild-type and in one case the resulting crystals yielded a diffraction pattern to 1.2 A resolution. This occurs in spite of the fact that mutating surface Glu residues almost invariably affects the protein's stability, as illustrated by the reduced deltaG between folded and unfolded forms measured by isothermal equilibrium denaturation. The present study strongly supports the notion that rational surface mutagenesis can be an effective tool in overcoming problems stemming from the protein's recalcitrance to crystallization and may also yield dramatic improvements in crystal quality.
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==About this Structure==
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1KMT is a [[Single protein]] structure of 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=1KMT OCA].
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==Reference==
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The impact of Glu--&gt;Ala and Glu--&gt;Asp mutations on the crystallization properties of RhoGDI: the structure of RhoGDI at 1.3 A resolution., Mateja A, Devedjiev Y, Krowarsch D, Longenecker K, Dauter Z, Otlewski J, Derewenda ZS, Acta Crystallogr D Biol Crystallogr. 2002 Dec;58(Pt 12):1983-91. Epub 2002, Nov 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12454455 12454455]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Dauter, Z.]]
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[[Category: Dauter Z]]
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[[Category: Derewenda, Z S.]]
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[[Category: Derewenda ZS]]
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[[Category: Devedjiev, Y.]]
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[[Category: Devedjiev Y]]
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[[Category: Krowarsh, D.]]
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[[Category: Krowarsh D]]
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[[Category: Longenecker, K.]]
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[[Category: Longenecker K]]
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[[Category: Mateja, A.]]
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[[Category: Mateja A]]
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[[Category: Otlewski, J.]]
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[[Category: Otlewski J]]
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[[Category: Beta sandwich motif]]
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[[Category: Immunoglobulin fold]]
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[[Category: Isoprenyl-binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:55:40 2008''
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Current revision

Crystal structure of RhoGDI Glu(154,155)Ala mutant

PDB ID 1kmt

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