1G2V

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

Summary for 1G2V

• Entry DOI: 10.2210/pdb1g2v/pdb
• Related: 1fxo 1fzw 1g0r 1g1l 1g23 1g31
• Descriptor: GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE, THYMIDINE-5'-TRIPHOSPHATE (2 entities in total)
• Functional Keywords: l-rhamnose, nucleotidyltransferase, pyrophosphorylase, thymidylyltransferase, allostery, transferase
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 8
• Total formula weight: 267625.44

Authors

Blankenfeldt, W.,Asuncion, M.,Lam, J.S.,Naismith, J.H. (deposition date: 2000-10-21, release date: 2000-12-27, Last modification date: 2023-08-09)

• Primary citation: Blankenfeldt, W.,Asuncion, M.,Lam, J.S.,Naismith, J.H.; The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate thymidylyltransferase (RmlA).; EMBO J., 19:6652-6663, 2000; PubMed: 11118200; DOI: 10.1093/emboj/19.24.6652

Experimental method

X-RAY DIFFRACTION (2.6 Å)