2p09: Difference between revisions

Revision as of 21:25, 27 July 2008

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File:2p09.png

2p09, resolution 1.65Å ()

Ligands:

, , ,

Related:

2p05

Resources:

FirstGlance, OCA, RCSB, PDBsum

Coordinates:

save as pdb, mmCIF, xml

Structural Insights into the Evolution of a Non-Biological ProteinStructural Insights into the Evolution of a Non-Biological Protein

Template:ABSTRACT PUBMED 17520026

About this StructureAbout this Structure

Full crystallographic information is available from OCA.

ReferenceReference

Structural insights into the evolution of a non-biological protein: importance of surface residues in protein fold optimization., Smith MD, Rosenow MA, Wang M, Allen JP, Szostak JW, Chaput JC, PLoS ONE. 2007 May 23;2(5):e467. PMID:17520026

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

OCA

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+===Structural Insights into the Evolution of a Non-Biological Protein===
-==Overview==
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-Phylogenetic profiling of amino acid substitution patterns in proteins has led many to conclude that most structural information is carried by interior core residues that are solvent inaccessible. This conclusion is based on the observation that buried residues generally tolerate only conserved sequence changes, while surface residues allow more diverse chemical substitutions. This notion is now changing as it has become apparent that both core and surface residues play important roles in protein folding and stability. Unfortunately, the ability to identify specific mutations that will lead to enhanced stability remains a challenging problem. Here we discuss two mutations that emerged from an in vitro selection experiment designed to improve the folding stability of a non-biological ATP binding protein. These mutations alter two solvent accessible residues, and dramatically enhance the expression, solubility, thermal stability, and ligand binding affinity of the protein. The significance of both mutations was investigated individually and together, and the X-ray crystal structures of the parent sequence and double mutant protein were solved to a resolution limit of 2.8 and 1.65 A, respectively. Comparative structural analysis of the evolved protein to proteins found in nature reveals that our non-biological protein evolved certain structural features shared by many thermophilic proteins. This experimental result suggests that protein fold optimization by in vitro selection offers a viable approach to generating stable variants of many naturally occurring proteins whose structures and functions are otherwise difficult to study.
+The line below this paragraph, {{ABSTRACT_PUBMED_17520026}}, adds the Publication Abstract to the page
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 [[Category: Wang, M.]]
 [[Category: Alpha/beta fold]]
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