4ECM

2.3 Angstrom Crystal Structure of a Glucose-1-phosphate Thymidylyltransferase from Bacillus anthracis in Complex with Thymidine-5-diphospho-alpha-D-glucose and Pyrophosphate

Summary for 4ECM

• Entry DOI: 10.2210/pdb4ecm/pdb
• Related: 3HL3
• Descriptor: Glucose-1-phosphate thymidylyltransferase, 2'DEOXY-THYMIDINE-5'-DIPHOSPHO-ALPHA-D-GLUCOSE, PYROPHOSPHATE 2-, ... (4 entities in total)
• Functional Keywords: glucose-1-phosphate thymidylyltransferase, transferase, structural genomics, center for structural genomics of infectious diseases, csgid
• Biological source: Bacillus anthracis (anthrax,anthrax bacterium)
• Total number of polymer chains: 1
• Total formula weight: 31018.60

Authors

Minasov, G.,Kuhn, M.,Halavaty, A.,Shuvalova, L.,Dubrovska, I.,Winsor, J.,Papazisi, L.,Anderson, W.F.,Center for Structural Genomics of Infectious Diseases (CSGID) (deposition date: 2012-03-26, release date: 2012-04-04, Last modification date: 2023-09-13)

Primary citation

Baumgartner, J.,Lee, J.,Halavaty, A.S.,Minasov, G.,Anderson, W.F.,Kuhn, M.L.
Structure of the Bacillus anthracis dTDP-L-rhamnose-biosynthetic enzyme glucose-1-phosphate thymidylyltransferase (RfbA).
Acta Crystallogr F Struct Biol Commun, 73:621-628, 2017

PubMed Abstract: L-Rhamnose is a ubiquitous bacterial cell-wall component. The biosynthetic pathway for its precursor dTDP-L-rhamnose is not present in humans, which makes the enzymes of the pathway potential drug targets. In this study, the three-dimensional structure of the first protein of this pathway, glucose-1-phosphate thymidylyltransferase (RfbA), from Bacillus anthracis was determined. In other organisms this enzyme is referred to as RmlA. RfbA was co-crystallized with the products of the enzymatic reaction, dTDP-α-D-glucose and pyrophosphate, and its structure was determined at 2.3 Å resolution. This is the first reported thymidylyltransferase structure from a Gram-positive bacterium. RfbA shares overall structural characteristics with known RmlA homologs. However, RfbA exhibits a shorter sequence at its C-terminus, which results in the absence of three α-helices involved in allosteric site formation. Consequently, RfbA was observed to exhibit a quaternary structure that is unique among currently reported glucose-1-phosphate thymidylyltransferase bacterial homologs. These structural analyses suggest that RfbA may not be allosterically regulated in some organisms and is structurally distinct from other RmlA homologs.

PubMed: 29095156
DOI: 10.1107/S2053230X17015357

Experimental method

X-RAY DIFFRACTION (2.3 Å)