3Q98

Structure of ygeW encoded protein from E. coli

Summary for 3Q98

• Entry DOI: 10.2210/pdb3q98/pdb
• Descriptor: transcarbamylase (2 entities in total)
• Functional Keywords: rossmann fold, unknown transcarbamylase, transferase
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 45228.09

Authors

Li, Y.,Jing, Z.,Yu, X.,Allewell, N.M.,Tuchman, M.,Shi, D. (deposition date: 2011-01-07, release date: 2011-05-04, Last modification date: 2024-11-20)

Primary citation

Li, Y.,Jin, Z.,Yu, X.,Allewell, N.M.,Tuchman, M.,Shi, D.
The ygeW encoded protein from Escherichia coli is a knotted ancestral catabolic transcarbamylase.
Proteins, 79:2327-2334, 2011

PubMed Abstract: The allantoin degradation pathway in has long been thought to involve a putative novel oxamate transcarbamylase (OXTCase) that converts oxaluric acid to oxamate and carbamyl phosphate (CP), a substrate for carbamate kinase (CK). In the genome sequence of , the only gene that could encode a novel transcarbamylase is the gene. However, the recombinant protein has no transcarbamylase activity with oxamate, allantoin, or twenty five other related compounds as potential substrates. The crystal structures of this transcarbamylase with unknown function (UTCase) has been determined and refined at 2.0 Å resolution, providing structural insights into its possible function. Like -acetyl-L-ornithine transcarbamylase and -succinyl-L-transcarbamylase, UTCase has a deep 3 trefoil knot close to the active site, in contrast to aspartate transcarbamylase and ornithine transcarbamylase which do not have a knot. A Blast search of completed genomes indicates that 52 species including one non-bacterial species, G3, have the gene. Gene context analysis and the structure of UTCase suggest that it is probably an ancestral catabolic transcarbamylase.

PubMed: 21557323
DOI: 10.1002/prot.23043

Experimental method

X-RAY DIFFRACTION (2.001 Å)