PDBsum entry: 2keq

Splicing

PDB-id: 2keq

Contents

Description

Header details

Header records

References

PROCHECK

Protein chain

139 a.a. *

* Residue conservation analysis

Tools

Clefts Calculation

PDB id:

2keq

Name:

Splicing

Title:

Solution structure of dnae intein from nostoc punctiforme

Structure:

DNA polymerase iii alpha subunit, nucleic acid binding ob-fold tRNA/helicase-type. Chain: a. Engineered: yes. Mutation: yes. Other_details: fusion protein of n-intein part from DNA polymerase iii alpha subunit (residues 1-102) and c-intein part from nucleic acid binding ob-fold, tRNA/helicase-type (residues 103-137)

Source:

Nostoc punctiforme pcc 73102. Organism_taxid: 63737. Gene: dnae, npun_f4872. Expressed in: escherichia coli. Expression_system_taxid: 562.

UniProt:

B2J066 (B2J066_NOSP7)

Seq:
Struc:
	Seq:
	Struc:
Seq:		876 a.a.
Struc:		139 a.a.*

B2J821 (B2J821_NOSP7)

Seq:

Struc:

Seq:

Struc:

Seq:

450 a.a.

Struc:

139 a.a.*

Key:	Secondary structure

* PDB and UniProt seqs differ at 4 residue positions (black crosses)

Enzyme class:

E.C.2.7.7.7   [IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

Reaction:

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1) (see diagram below)

Resolution:

not givenÅ

NMR structure:

20 models

Authors:

J.S.Oeemig,A.S.Aranko,J.B.Djupsj,H.Iwai

Key ref:

J.S.Oeemig et al. (2009). Solution structure of DnaE intein from Nostoc punctiforme: structural basis for the design of a new split intein suitable for site-specific chemical modification.. Febs Lett, 583, 1451-1456. [PubMed id: 19344715] [DOI: 10.1016/j.febslet.2009.03.058]

Date:

02-Feb-09

Release date:

19-May-09

Related entries:

16009 related db: bmrb
entry contains the specific resonance assignment of npudnae
intein from nostoc punctiforme

Quick_links

Procheck

Clefts

Surface

Key reference

DOI no: 10.1016/j.febslet.2009.03.058

Febs Lett 583:1451-1456 (2009)

PubMed id: 19344715

Solution structure of DnaE intein from Nostoc punctiforme: structural basis for the design of a new split intein suitable for site-specific chemical modification.

J.S.Oeemig, A.S.Aranko, J.Djupsjöbacka, K.Heinämäki, H.Iwaï.

ABSTRACT

Naturally split DnaE intein from Nostoc punctiforme (Npu) has robust protein trans-splicing activity and high tolerance of sequence variations at the splicing junctions. We determined the solution structure of a single chain variant of NpuDnaE intein by NMR spectroscopy. Based on the NMR structure and the backbone dynamics of the single chain NpuDnaE intein, we designed a functional split variant of the NpuDnaE intein having a short C-terminal half (C-intein) composed of six residues. In vivo and in vitro protein ligation of model proteins by the newly designed split intein were demonstrated.