PubMed Health⌕ Search
Home/Archive/PubMed

PubMed · 15604105

Structural drift: a possible path to protein fold change.

S Sri Krishna·Nick V Grishin
View original source ↗Export metadata ↓

Abstract

SUMMARY: Along with their mutating sequences, protein structures change in time. Analyzing a formate dehydrogenase domain that is evolutionarily related to ferredoxin, but simultaneously contains all the structural elements of a beta-Grasp fold, we illustrate here a mechanism termed as structural drift, by which changes to a protein fold can occur. CONTACT: grishin@chop.swmed.edu.

Explore related subjects

Carrier ProteinsEvolution, MolecularFerredoxinsFormate DehydrogenasesGenetic DriftMembrane ProteinsModels, ChemicalModels, MolecularProtein FoldingProtein Structure, TertiaryProtein SubunitsSequence Analysis, ProteinStructure-Activity RelationshipJournal ArticleResearch Support, N.I.H., ExtramuralResearch Support, U.S. Gov't, P.H.S.

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

S Sri Krishna, Nick V Grishin. 2004-12-16. Structural drift: a possible path to protein fold change.. https://doi.org/10.1093/bioinformatics%2Fbti227

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed2007

Electrochemical screening of recombinant protein solubility in Escherichia coli using scanning electrochemical microscopy (SECM).

A microbial array chip with collagen gel spots entrapping living Escherichia coli (E. coli) DH5alpha was applied for the screening of recombinant protein solubilities. The alpha-fragment of beta-galactosidase (betaGal) was fused to the target protein, namely, maltose-binding protein (MBP), to monitor the solubility of MBP. Scanning electrochemical microscopy (SECM) was used to detect the release of p-aminophenol from E. coli cells catalyzed by intracellular betaGal. Comparison of the SECM-based method with the Western blotting-based method indicated that the current response obtained using SECM increased with an increase in the betaGal activity and therefore, with the soluble fraction of MBP in the host cells.

Carrier Proteins↗
PubMed2007

Direct interactions between NEDD8 and ubiquitin E2 conjugating enzymes upregulate cullin-based E3 ligase activity.

Although cullin-1 neddylation is crucial for the activation of SCF ubiquitin E3 ligases, the underlying mechanisms for NEDD8-mediated activation of SCF remain unclear. Here we demonstrate by NMR and mutational studies that NEDD8 binds the ubiquitin E2 (UBC4), but not NEDD8 E2 (UBC12). Our data imply that NEDD8 forms an active platform on the SCF complex for selective recruitment of ubiquitin-charged E2s in collaboration with RBX1, and thereby upregulates the E3 activity.

Carrier Proteins↗