1q4e: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1q4e.jpg|left|200px]] | [[Image:1q4e.jpg|left|200px]] | ||
'''S65T Q80R Y145C Green Fluorescent Protein (GFP) pH 8.5''' | {{Structure | ||
|PDB= 1q4e |SIZE=350|CAPTION= <scene name='initialview01'>1q4e</scene>, resolution 1.38Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''S65T Q80R Y145C Green Fluorescent Protein (GFP) pH 8.5''' | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
1Q4E is a [ | 1Q4E is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aequorea_victoria Aequorea victoria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q4E OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/14684834 14684834] | ||
[[Category: Aequorea victoria]] | [[Category: Aequorea victoria]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 20: | Line 29: | ||
[[Category: green fluorescent protein]] | [[Category: green fluorescent protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:32:58 2008'' | ||
Revision as of 14:32, 20 March 2008
| |||||||
| , resolution 1.38Å | |||||||
|---|---|---|---|---|---|---|---|
| Coordinates: | save as pdb, mmCIF, xml | ||||||
S65T Q80R Y145C Green Fluorescent Protein (GFP) pH 8.5
OverviewOverview
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.
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 Thu Mar 20 13:32:58 2008