THE STRUCTURAL BASIS OF THE CATALYTIC MECHANISM AND REGULATION OF GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE (RMLA). APO ENZYME.

The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate thymidylyltransferase (RmlA).

The Purification, Crystallisation and Preliminary Structural Characterisation of Glucose-1-phosphate Thymidylyltransferase (RmlA), the First Enzyme of the dTDP-L-rhamnose Synthesis Pathway from Pseudomonas aeruginosa

The Nucleotide Specificity and Feedback Control of Thymidine Diphosphate D-glucose Pyrophosphorylase

GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE

GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE (RMLA)

0.1 M Na-citrate,
0.5 M Li-sulfate,
9-11% (w/v) PEG 6000, pH 4.6, VAPOR DIFFUSION, SITTING DROP, temperature 292K

1fxo is RmlA in complex with 2'-deoxy-thymidine-5'-monophosphate (TMP)

1g0r is RmlA in complex with 2'-deoxy-thimidine (THM) and alpha-D-glucose-1-phosphate (G1P)

1g1l is RmlA in complex with 2'-deoxy-thymidine-alpha-D-glucose (TDG)

1g23 is RmlA in complex with alpha-D-glucose-1-phosphate (G1P)

1g2v is RmlA in complex with 2'-deoxy-thymidine-5'-triphosphate (TTP)

1g31 is RmlA in complex with 2'-deoxy-thymidine-beta-L-rhamnose (TDR)

GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE (E.C.2.7.7.24)
The biological assembly is a tetramer that can be described as a dimer of dimers
rhamnose, nucleotidyltransferase, pyrophosphorylase, thymidylyltransferase, allostery, TRANSFERASE