1q4e: Difference between revisions

Revision as of 12:51, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1q4e.png

Template:STRUCTURE 1q4e

S65T Q80R Y145C Green Fluorescent Protein (GFP) pH 8.5S65T Q80R Y145C Green Fluorescent Protein (GFP) pH 8.5

Template:ABSTRACT PUBMED 14684834

About this StructureAbout this Structure

1Q4E is a Single protein structure of sequence from Aequorea victoria. Full crystallographic information is available from OCA.

ReferenceReference

Local complexity of amino acid interactions in a protein core., Jain RK, Ranganathan R, Proc Natl Acad Sci U S A. 2004 Jan 6;101(1):111-6. Epub 2003 Dec 18. PMID:14684834

Page seeded by OCA on Mon Jul 28 12:50:59 2008

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OCA

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-==Overview==
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-Atomic resolution structures of proteins indicate that the core is typically well packed, suggesting a densely connected network of interactions between amino acid residues. The combinatorial complexity of energetic interactions in such a network could be enormous, a problem that limits our ability to relate structure and function. Here, we report a case study of the complexity of amino acid interactions in a localized region within the core of the GFP, a particularly stable and tightly packed molecule. Mutations at three sites within the chromophore-binding pocket display an overlapping pattern of conformational change and are thermodynamically coupled, seemingly consistent with the dense network model. However, crystallographic and energetic analyses of coupling between mutations paint a different picture; pairs of mutations couple through independent "hotspots" in the region of structural overlap. The data indicate that, even in highly stable proteins, the core contains sufficient plasticity in packing to uncouple high-order energetic interactions of residues, a property that is likely general in proteins.
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