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Role of structural determinants in folding of the sandwich-like protein Pseudomonas aeruginosa azurin.

Abstract：

:An invariant substructure that forms two interlocked pairs of neighboring beta-strands occurs in essentially all known sandwich-like proteins. Eight conserved positions in these strands were recently shown to act as structural determinants. To test whether the residues at these invariant positions are conserved for mechanistic (i.e., part of folding nucleus) or energetic (i.e., governing native-state stability) reasons, we characterized the folding behavior of eight point-mutated variants of the sandwich-like protein Pseudomonas aeruginosa apo-azurin. We find a simple relationship among the conserved positions: half of the residues form native-like interactions in the folding transition state, whereas the others do not participate in the folding nucleus but govern high native-state stability. Thus, evolutionary preservation of these specific positions gives both mechanistic and energetic advantages to members of the sandwich-like protein family.

journal_name

Proc Natl Acad Sci U S A

journal_title

Proceedings of the National Academy of Sciences of the United States of America

authors

Wilson CJ,Wittung-Stafshede P

doi

10.1073/pnas.0501038102

keywords:

subject

Has Abstract

pub_date

2005-03-15 00:00:00

pages

3984-7

issue

11

eissn

0027-8424

issn

1091-6490

pii

0501038102

journal_volume

102

pub_type

杂志文章

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