PDBsum entry: 1imo

Ligase

PDB id: 1imo

Contents

Protein chain

88 a.a. *

* Residue conservation analysis

PDB id:

1imo

Name:

Ligase

Title:

Nmr structure of human DNA ligase iiialpha brct domain

Structure:

DNA ligase iii. Chain: a. Fragment: brct domain. Synonym: polydeoxyribonucleotide synthase [atp]. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

1 models

Authors:

V.V.Krishnan,K.H.Thornton,M.P.Thelen,M.Cosman

Key ref:

V.V.Krishnan et al. (2001). Solution structure and backbone dynamics of the human DNA ligase IIIalpha BRCT domain. Biochemistry, 40, 13158-13166. PubMed id: 11683624 DOI: 10.1021/bi010979g

Date:

11-May-01 Release date: 25-May-01

Protein chain

P49916  (DNLI3_HUMAN) -  DNA ligase 3

Seq: 1009 a.a.

Struc: 88 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.6.5.1.1 - Dna ligase (ATP).
• Reaction: ATP + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + diphosphate + (deoxyribonucleotide)(n+m)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 Gene Ontology (GO) functional annotation 

• Cellular component: intracellular (1 term)

reference

DOI no: 10.1021/bi010979g

Biochemistry 40:13158-13166 (2001)

PubMed id: 11683624

Solution structure and backbone dynamics of the human DNA ligase IIIalpha BRCT domain.

V.V.Krishnan, K.H.Thornton, M.P.Thelen, M.Cosman.

ABSTRACT

BRCT (BRCA1 carboxyl terminus) domains are found in a number of DNA repair enzymes and cell cycle regulators and are believed to mediate important protein-protein interactions. The DNA ligase IIIalpha BRCT domain partners with the distal BRCT domain of the DNA repair protein XRCC1 (X1BRCTb) in the DNA base excision repair (BER) pathway. To elucidate the mechanisms by which these two domains can interact, we have determined the solution structure of human ligase consists of a beta2beta1beta3beta4 parallel sheet with a two-alpha-helix bundle packed against one face of the sheet. This fold is conserved in several proteins having a wide range of activities, including X1BRCTb [Zhang, X. D., et al. (1998) EMBO J. 17, exists as a dimer in solution, but an insufficient number of NOE restraints precluded the determination of the homodimer structure. However, 13C isotope-filtered and hydrogen-deuterium exchange experiments indicate that the N-terminus, alpha1, the alpha1-beta2 loop, and the three residues following alpha2 are involved in forming the dimer interface, as similarly observed in the structure of X1BRCTb. NOE and dynamic data indicate that several residues (837-844) in the N-terminal region appear to interconvert between helix and random coil conformations. Further studies of other BRCT domains and of their complexes are needed to address how these proteins interact with one another, and to shed light on how mutations can lead to disruption of function and ultimately disease.