1E3H

SeMet derivative of Streptomyces antibioticus PNPase/GPSI enzyme

Summary for 1E3H

Entry DOI	10.2210/pdb1e3h/pdb
Related	1E3P
Descriptor	GUANOSINE PENTAPHOSPHATE SYNTHETASE, SULFATE ION (3 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	83027.86
Authors	Symmons, M.F.,Jones, G.H.,Luisi, B.F. (deposition date: 2000-06-15, release date: 2000-11-05, Last modification date: 2024-10-23)
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 (2.6 Å)

Structure validation