1q4b

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[[Image:1q4b.gif|left|200px]]
[[Image:1q4b.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1q4b |SIZE=350|CAPTION= <scene name='initialview01'>1q4b</scene>, resolution 1.48&Aring;
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The line below this paragraph, containing "STRUCTURE_1q4b", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CRO:[2-(1-AMINO-2-HYDROXY-PROPYL)-4-(4-HYDROXY-BENZYLIDINE)-5-OXO-4,5-DIHYDRO-IMIDAZOL-1-YL]-ACETALDEHYDE'>CRO</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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|GENE=
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{{STRUCTURE_1q4b| PDB=1q4b | SCENE= }}
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|RELATEDENTRY=[[1q4a|1Q4A]], [[1q4c|1Q4C]], [[1q4d|1Q4D]], [[1q4e|1Q4E]], [[1q73|1Q73]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1q4b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q4b OCA], [http://www.ebi.ac.uk/pdbsum/1q4b PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1q4b RCSB]</span>
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}}
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'''S65T Q80R Green Fluorescent Protein (GFP) pH 5.5'''
'''S65T Q80R Green Fluorescent Protein (GFP) pH 5.5'''
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[[Category: Jain, R K.]]
[[Category: Jain, R K.]]
[[Category: Ranganathan, R.]]
[[Category: Ranganathan, R.]]
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[[Category: chromophore]]
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[[Category: Chromophore]]
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[[Category: fluorophore]]
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[[Category: Fluorophore]]
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[[Category: gfp]]
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[[Category: Gfp]]
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[[Category: green fluorescent protein]]
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[[Category: Green fluorescent protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:51:11 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:08:39 2008''
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Revision as of 02:51, 3 May 2008

Template:STRUCTURE 1q4b

S65T Q80R Green Fluorescent Protein (GFP) pH 5.5


Overview

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 Structure

1Q4B is a Single protein structure of sequence from Aequorea victoria. Full crystallographic information is available from OCA.

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:14684834 Page seeded by OCA on Sat May 3 05:51:11 2008

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