1QSL

KLENOW FRAGMENT COMPLEXED WITH SINGLE-STRANDED SUBSTRATE AND EUROPIUM (III) ION

Summary for 1QSL

• Entry DOI: 10.2210/pdb1qsl/pdb
• Descriptor: 5'-D(*GP*CP*TP*TP*AP*CP*GP*C)-3', DNA POLYMERASE I, EUROPIUM ION, ... (4 entities in total)
• Functional Keywords: exonuclease, two metal ions, single-stranded dna, transferase/dna, transferase-dna complex
• Biological source: Escherichia coli; More
• Total number of polymer chains: 2
• Total formula weight: 70748.31

Authors

Brautigam, C.A.,Aschheim, K.,Steitz, T.A. (deposition date: 1999-06-22, release date: 1999-06-30, Last modification date: 2024-02-14)

Primary citation

Brautigam, C.A.,Aschheim, K.,Steitz, T.A.
Structural elucidation of the binding and inhibitory properties of lanthanide (III) ions at the 3'-5' exonucleolytic active site of the Klenow fragment
Chem.Biol., 6:901-908, 1999

PubMed Abstract: Biochemical and biophysical experiments have shown that two catalytically essential divalent metal ions (termed 'A' and 'B') bind to the 3'-5' exonuclease active site of the Klenow fragment (KF) of Escherichia coli DNA polymerase I. X-ray crystallographic studies have established the normal positions in the KF 3'-5' exonuclease (KF exo) active site of the two cations and the single-stranded DNA substrate. Lanthanide (III) luminescence studies have demonstrated, however, that only a single europium (III) ion (Eu3+) binds to the KF exo active site. Furthermore, Eu3+ does not support catalysis by KF exo or several other two-metal-ion phosphoryl-transfer enzymes.

PubMed: 10631518
DOI: 10.1016/S1074-5521(00)80009-5

Experimental method

X-RAY DIFFRACTION (2.2 Å)