1E3P

tungstate derivative of Streptomyces antibioticus PNPase/GPSI enzyme

Summary for 1E3P

Entry DOI	10.2210/pdb1e3p/pdb
Related	1E3H
Descriptor	Polyribonucleotide nucleotidyltransferase, SULFATE ION, TUNGSTATE(VI)ION, ... (4 entities in total)
Functional Keywords	polyribonucleotide transferase, atp-gtp diphosphotransferase rna processing, rna degradation
Biological source	Streptomyces antibioticus
Total number of polymer chains	1
Total formula weight	82433.84
Authors	Symmons, M.F.,Jones, G.H.,Luisi, B.F. (deposition date: 2000-06-20, release date: 2000-11-03, Last modification date: 2023-12-13)
Primary citation	Symmons, M.F.,Jones, G.H.,Luisi, B.F. A Duplicated Fold is the Structural Basis for Polynucleotide Phosphorylase Catalytic Activity, Processivity, and Regulation Structure, 8:1215-, 2000 Cited by PubMed Abstract: Polynucleotide phosphorylase (PNPase) is a polyribonucleotide nucleotidyl transferase (E.C.2.7.7.8) that degrades mRNA in prokaryotes. Streptomyces antibioticus PNPase also assays as a guanosine 3'-diphosphate 5'-triphosphate (pppGpp) synthetase (E.C.2.7.6.5). It may function to coordinate changes in mRNA lifetimes with pppGpp levels during the Streptomyces lifecycle. PubMed: 11080643 DOI: 10.1016/S0969-2126(00)00521-9 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.5 Å)

Structure validation