1ft0: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
New page: left|200px<br /> <applet load="1ft0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ft0, resolution 2.6Å" /> '''CRYSTAL STRUCTURE OF...
 
No edit summary
 
(17 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1ft0.gif|left|200px]]<br />
<applet load="1ft0" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1ft0, resolution 2.6&Aring;" />
'''CRYSTAL STRUCTURE OF TRUNCATED HUMAN RHOGDI K113A MUTANT'''<br />


==Overview==
==CRYSTAL STRUCTURE OF TRUNCATED HUMAN RHOGDI K113A MUTANT==
Crystallization is a unique process that occurs at the expense of entropy, including the conformational entropy of surface residues, which become, ordered in crystal lattices during formation of crystal contacts. It could, therefore be argued that epitopes free of amino acids with high, conformational entropy are more thermodynamically favorable for crystal, formation. For a protein recalcitrant to crystallization, mutation of such, surface amino acids to residues with no conformational entropy might lead, to enhancement of crystallization. This paper reports the results of, experiments with an important cytosolic regulator of GTPases, human, RhoGDI, in which lysine residues were systematically mutated to alanines., Single and multiple mutations were introduced into two different variants, of RhoGDI, NDelta23 and NDelta66, in which the first 23 and 66 residues, respectively, were removed by recombinant methods. In total, 13 single and, multiple mutants were prepared and assessed for crystallization and all, were shown to crystallize using the Hampton Research Crystal Screens I and, II, in contrast to wild-type NDelta23 and NDelta66 RhoGDI which did not, crystallize. Four crystal structures were solved (the triple mutants, NDelta23:K135,138,141A and NDelta66:K135,138,141A, and two single mutants, NDelta66:K113A and NDelta66:K141A) and in three cases the crystal contacts, of the new lattices were found precisely at the sites of mutations. These, results support the notion that it is, in principle, possible to, rationally design mutations which systematically enhance proteins' ability, to crystallize.
<StructureSection load='1ft0' size='340' side='right'caption='[[1ft0]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ft0]] 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=1FT0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FT0 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</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=1ft0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ft0 OCA], [https://pdbe.org/1ft0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ft0 RCSB], [https://www.ebi.ac.uk/pdbsum/1ft0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ft0 ProSAT]</span></td></tr>
</table>
== Function ==
[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).
== 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/ft/1ft0_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/main_output.php?pdb_ID=1ft0 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1FT0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FT0 OCA].
*[[Guanine nucleotide dissociation inhibitor|Guanine nucleotide dissociation inhibitor]]
 
__TOC__
==Reference==
</StructureSection>
Protein crystallization by rational mutagenesis of surface residues: Lys to Ala mutations promote crystallization of RhoGDI., Longenecker KL, Garrard SM, Sheffield PJ, Derewenda ZS, Acta Crystallogr D Biol Crystallogr. 2001 May;57(Pt 5):679-88. Epub 2001, Apr 24. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11320308 11320308]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Derewenda, Z.S.]]
[[Category: Derewenda ZS]]
[[Category: Garrard, S.M.]]
[[Category: Garrard SM]]
[[Category: Longenecker, K.L.]]
[[Category: Longenecker KL]]
[[Category: Sheffield, P.J.]]
[[Category: Sheffield PJ]]
[[Category: beta sandwich motif]]
[[Category: gdp-dissociation inhibitor of rho gtpases]]
[[Category: immunoglobulin fold]]
[[Category: isoprenyl-binding domain]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:57:07 2007''

Latest revision as of 10:19, 7 February 2024

CRYSTAL STRUCTURE OF TRUNCATED HUMAN RHOGDI K113A MUTANTCRYSTAL STRUCTURE OF TRUNCATED HUMAN RHOGDI K113A MUTANT

Structural highlights

1ft0 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 2.6Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).

Evolutionary Conservation

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

See Also

1ft0, resolution 2.60Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=1ft0&oldid=4043780"