Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6TH8

Reconstructing the Origins of the HemD-like fold

Summary for 6TH8
Entry DOI10.2210/pdb6th8/pdb
NMR InformationBMRB: 34452
DescriptorcU3Sd (1 entity in total)
Functional Keywordsprotein design, hemd-like fold, flavodoxin-like fold, flavoprotein
Biological sourceThermus thermophilus
Total number of polymer chains1
Total formula weight13651.65
Authors
Coles, M.,Toledo-Patino, S.,Chaubey, M.,Hocker, B. (deposition date: 2019-11-19, release date: 2019-11-27, Last modification date: 2024-06-19)
Primary citationToledo-Patino, S.,Chaubey, M.,Coles, M.,Hocker, B.
Reconstructing the Remote Origins of a Fold Singleton from a Flavodoxin-Like Ancestor.
Biochemistry, 58:4790-4793, 2019
Cited by
PubMed Abstract: Evolutionary processes that led to the emergence of structured protein domains left footprints in the sequences of modern proteins. We searched for such hints employing state-of-the-art sequence analysis and found evidence that the HemD-like fold emerged from the flavodoxin-like fold through segment swap and gene duplication. To verify this hypothesis, we reverted these evolutionary steps experimentally, constructing a HemD-half that resulted in a protein with the canonical flavodoxin-like architecture. These results of fold reconstruction from the sequence of a different fold strongly support our hypothesis of common ancestry. It further illustrates the plasticity of modern proteins to form new folded proteins.
PubMed: 31724394
DOI: 10.1021/acs.biochem.9b00900
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

227344

PDB entries from 2024-11-13

PDB statisticsPDBj update infoContact PDBjnumon