Abstract
Our investigation of knotted structures in the Protein Data Bank reveals the most complicated knot discovered to date. We suggest that the occurrence of this knot in a human ubiquitin hydrolase might be related to the role of the enzyme in protein degradation. While knots are usually preserved among homologues, we also identify an exception in a transcarbamylase. This allows us to exemplify the function of knots in proteins and to suggest how they may have been created.
Publication types
-
Research Support, Non-U.S. Gov't
-
Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
-
Bacterial Proteins / chemistry
-
Bacterial Proteins / genetics
-
Bacterial Proteins / metabolism
-
Computational Biology
-
Cysteine Endopeptidases / chemistry*
-
Cysteine Endopeptidases / genetics
-
Cysteine Endopeptidases / metabolism*
-
Databases, Genetic
-
Evolution, Molecular*
-
Humans
-
Models, Molecular
-
Protein Binding
-
Protein Structure, Tertiary
-
Ubiquitin Thiolesterase
Substances
-
Bacterial Proteins
-
UCHL3 protein, human
-
Ubiquitin Thiolesterase
-
Cysteine Endopeptidases
Associated data
-
PDB/1A1S
-
PDB/1C9Y
-
PDB/1CMX
-
PDB/1FUG
-
PDB/1JS1
-
PDB/1P35
-
PDB/1QM4
-
PDB/1XD3
-
PDB/1YH1
-
PDB/1YRL
-
PDB/1YVE
-
PDB/1ZTU
-
PDB/2BTV
-
PDB/2ETL