2j5a: Difference between revisions

Revision as of 14:35, 27 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:2j5a.png

Template:STRUCTURE 2j5a

FOLDING OF S6 STRUCTURES WITH DIVERGENT AMINO-ACID COMPOSITION: PATHWAY FLEXIBILITY WITHIN PARTLY OVERLAPPING FOLDONSFOLDING OF S6 STRUCTURES WITH DIVERGENT AMINO-ACID COMPOSITION: PATHWAY FLEXIBILITY WITHIN PARTLY OVERLAPPING FOLDONS

Template:ABSTRACT PUBMED 17056063

About this StructureAbout this Structure

2J5A is a Single protein structure of sequence from Aquifex aeolicus. Full crystallographic information is available from OCA.

ReferenceReference

Folding of S6 structures with divergent amino acid composition: pathway flexibility within partly overlapping foldons., Olofsson M, Hansson S, Hedberg L, Logan DT, Oliveberg M, J Mol Biol. 2007 Jan 5;365(1):237-48. Epub 2006 Sep 12. PMID:17056063

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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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-[[Image:2j5a.gif|left|200px]]
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 {{STRUCTURE_2j5a|  PDB=2j5a  |  SCENE=  }}
-'''FOLDING OF S6 STRUCTURES WITH DIVERGENT AMINO-ACID COMPOSITION: PATHWAY FLEXIBILITY WITHIN PARTLY OVERLAPPING FOLDONS'''
+===FOLDING OF S6 STRUCTURES WITH DIVERGENT AMINO-ACID COMPOSITION: PATHWAY FLEXIBILITY WITHIN PARTLY OVERLAPPING FOLDONS===
-==Overview==
+<!--
-Studies of circular permutants have demonstrated that the folding reaction of S6 from Thermus thermophilus (S6(T)) is malleable and responds in an ordered manner to changes of the sequence separation between interacting residues: the S6(T) permutants retain a common nucleation pattern in the form of a two-strand-helix motif that can be recruited from different parts of the structure. To further test the robustness of the two-strand-helix nucleus we have here determined the crystal structure and folding reaction of an evolutionary divergent S6 protein from the hyperthermophilic bacterium Aquifex aeolicus (S6(A)). Although the overall topology of S6(A) is very similar to that of S6(T) the architecture of the hydrophobic core is radically different by containing a large proportion of stacked Phe side-chains. Despite this disparate core composition, the folding rate constant and the kinetic m values of S6(A) are identical to those of S6(T). The folding nucleus of S6(A) is also found to retain the characteristic two-strand-helix motif of the S6(T) permutants, but with a new structural emphasis. The results suggest that the protein folding reaction is linked to topology only in the sense that the native-state topology determines the repertoire of accessible nucleation motifs. If the native structure allows several equivalent ways of recruiting a productive nucleus the folding reaction is free to redistribute within these topological constraints.
+The line below this paragraph, {{ABSTRACT_PUBMED_17056063}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17056063 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_17056063}}
 ==About this Structure==
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 [[Category: Ribosomal protein s6,rna-binding]]
 [[Category: Rrna-binding]]
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