2j5a
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(New page: 200px<br /> <applet load="2j5a" size="450" color="white" frame="true" align="right" spinBox="true" caption="2j5a, resolution 2.300Å" /> '''FOLDING OF S6 STRU...)
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Revision as of 16:00, 29 October 2007
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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, ... [(full description)]
About this Structure
2J5A is a [Single protein] structure of sequence from [Aquifex aeolicus] with NA as [ligand]. Full crystallographic information is available from [OCA].
Reference
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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