From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1ft0.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1ft0.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1ft0| PDB=1ft0 | SCENE= }} | | {{STRUCTURE_1ft0| PDB=1ft0 | SCENE= }} |
| | | | |
| - | '''CRYSTAL STRUCTURE OF TRUNCATED HUMAN RHOGDI K113A MUTANT'''
| + | ===CRYSTAL STRUCTURE OF TRUNCATED HUMAN RHOGDI K113A MUTANT=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11320308}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11320308 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_11320308}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 30: |
Line 34: |
| | [[Category: Immunoglobulin fold]] | | [[Category: Immunoglobulin fold]] |
| | [[Category: Isoprenyl-binding domain]] | | [[Category: Isoprenyl-binding domain]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:43:59 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:54:12 2008'' |
Revision as of 00:54, 1 July 2008
Template:STRUCTURE 1ft0
CRYSTAL STRUCTURE OF TRUNCATED HUMAN RHOGDI K113A MUTANT
Template:ABSTRACT PUBMED 11320308
About this Structure
1FT0 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Tue Jul 1 03:54:12 2008
