PDBsum entry 5aoy

Hydrolase

PDB id: 5aoy

Contents

Protein chain

239 a.a.

Waters ×302

PDB id:

5aoy

Name:

Hydrolase

Title:

Structure of mouse endonuclease v

Structure:

Endonuclease v. Chain: a. Engineered: yes. Mutation: yes

Source:

Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: codon plus ripl.

Resolution:

1.75Å R-factor: 0.166 R-free: 0.190

Authors:

E.S.Vik,M.S.Nawaz,M.E.Ronander,A.M.Solvoll,P.Strom-Andersen,M.Bjoras, I.Alseth,B.Dalhus

Key ref:

M.S.Nawaz et al. (2016). Crystal structure and MD simulation of mouse EndoV reveal wedge motif plasticity in this inosine-specific endonuclease. Sci Rep, 6, 24979. PubMed id: 27108838 DOI: 10.1038/srep24979

Date:

14-Sep-15 Release date: 04-May-16

Protein chain

Q8C9A2  (ENDOV_MOUSE) -  Endonuclease V from Mus musculus

Seq: 338 a.a.

Struc: 239 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.3.1.26.- - ?????

DOI no: 10.1038/srep24979

Sci Rep 6:24979 (2016)

PubMed id: 27108838

Crystal structure and MD simulation of mouse EndoV reveal wedge motif plasticity in this inosine-specific endonuclease.

M.S.Nawaz, E.S.Vik, M.E.Ronander, A.M.Solvoll, P.Blicher, M.Bjørås, I.Alseth, B.Dalhus.

ABSTRACT

Endonuclease V (EndoV) is an enzyme with specificity for deaminated adenosine (inosine) in nucleic acids. EndoV from Escherichia coli (EcEndoV) acts both on inosines in DNA and RNA, whereas the human homolog cleaves only at inosines in RNA. Inosines in DNA are mutagenic and the role of EndoV in DNA repair is well established. In contrast, the biological function of EndoV in RNA processing is largely unexplored. Here we have characterized a second mammalian EndoV homolog, mouse EndoV (mEndoV), and show that mEndoV shares the same RNA selectivity as human EndoV (hEndoV). Mouse EndoV cleaves the same inosine-containing substrates as hEndoV, but with reduced efficiencies. The crystal structure of mEndoV reveals a conformation different from the hEndoV and prokaryotic EndoV structures, particularly for the conserved tyrosine in the wedge motif, suggesting that this strand separating element has some flexibility. Molecular dynamics simulations of mouse and human EndoV reveal alternative conformations for the invariant tyrosine. The configuration of the active site, on the other hand, is very similar between the prokaryotic and mammalian versions of EndoV.