1EKE

CRYSTAL STRUCTURE OF CLASS II RIBONUCLEASE H (RNASE HII) WITH MES LIGAND

Summary for 1EKE

• Entry DOI: 10.2210/pdb1eke/pdb
• Descriptor: RIBONUCLEASE HII, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID (3 entities in total)
• Functional Keywords: nuclease, endonuclease, structural genomics, bsgc structure funded by nih, protein structure initiative, psi, berkeley structural genomics center, hydrolase
• Biological source: Methanocaldococcus jannaschii
• Cellular location: Cytoplasm (Potential): Q57599
• Total number of polymer chains: 2
• Total formula weight: 53777.69

Authors

Lai, L.H.,Yokota, H.,Hung, L.W.,Kim, R.,Kim, S.H.,Berkeley Structural Genomics Center (BSGC) (deposition date: 2000-03-07, release date: 2000-09-13, Last modification date: 2024-11-06)

Primary citation

Lai, L.,Yokota, H.,Hung, L.W.,Kim, R.,Kim, S.H.
Crystal structure of archaeal RNase HII: a homologue of human major RNase H
Structure, 8:897-904, 2000

PubMed Abstract: RNases H are present in all organisms and cleave RNAs in RNA/DNA hybrids. There are two major types of RNases H that have little similarity in sequence, size and specificity. The structure of RNase HI, the smaller enzyme and most abundant in bacteria, has been extensively studied. However, no structural information is available for the larger RNase H, which is most abundant in eukaryotes and archaea. Mammalian RNase H participates in DNA replication, removal of the Okazaki fragments and possibly DNA repair.

PubMed: 10997908
DOI: 10.1016/S0969-2126(00)00179-9

Experimental method

X-RAY DIFFRACTION (2 Å)