1ft3: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ft3]] is a 2 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=1FT3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FT3 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1ft3]] is a 2 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=1FT3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FT3 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fso|1fso]], [[1fst|1fst]], [[1ft0|1ft0]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fso|1fso]], [[1fst|1fst]], [[1ft0|1ft0]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ft3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ft3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ft3 RCSB], [http://www.ebi.ac.uk/pdbsum/1ft3 PDBsum]</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=1ft3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ft3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ft3 RCSB], [http://www.ebi.ac.uk/pdbsum/1ft3 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Derewenda, Z S | [[Category: Derewenda, Z S]] | ||
[[Category: Garrard, S M | [[Category: Garrard, S M]] | ||
[[Category: Longenecker, K L | [[Category: Longenecker, K L]] | ||
[[Category: Sheffield, P J | [[Category: Sheffield, P J]] | ||
[[Category: Beta sandwich motif]] | [[Category: Beta sandwich motif]] | ||
[[Category: Gdp-dissociation inhibitor of rho gtpase]] | [[Category: Gdp-dissociation inhibitor of rho gtpase]] | ||
Revision as of 01:14, 23 December 2014
CRYSTAL STRUCTURE OF TRUNCATED RHOGDI K141A MUTANTCRYSTAL STRUCTURE OF TRUNCATED RHOGDI K141A MUTANT
Structural highlights
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 PubMedCrystallization 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. 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:11320308[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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