PDBsum entry: 1bkn

DNA repair

PDB id: 1bkn

Contents

Protein chains

272 a.a. *

Waters ×55

* Residue conservation analysis

PDB id:

1bkn

Name:

DNA repair

Title:

Crystal structure of an n-terminal 40kd fragment of e. Coli DNA mismatch repair protein mutl

Structure:

Mutl. Chain: a, b. Fragment: n-terminal 40kd fragment. Engineered: yes

Source:

Escherichia coli k12. Organism_taxid: 83333. Strain: k-12. Gene: mutl. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.90Å R-factor: 0.248 R-free: 0.300

Authors:

W.Yang,C.Ban

Key ref:

C.Ban and W.Yang (1998). Crystal structure and ATPase activity of MutL: implications for DNA repair and mutagenesis. Cell, 95, 541-552. PubMed id: 9827806 DOI: 10.1016/S0092-8674(00)81621-9

Date:

09-Jul-98 Release date: 11-May-99

Protein chains

P23367  (MUTL_ECOLI) -  DNA mismatch repair protein mutL

Seq: 615 a.a.

Struc: 272 a.a.

 Gene Ontology (GO) functional annotation 

• Biological process: mismatch repair (1 term)
• Biochemical function: ATP binding (2 terms)

DOI no: 10.1016/S0092-8674(00)81621-9

Cell 95:541-552 (1998)

PubMed id: 9827806

Crystal structure and ATPase activity of MutL: implications for DNA repair and mutagenesis.

C.Ban, W.Yang.

ABSTRACT

MutL and its homologs are essential for DNA mismatch repair. Mutations in genes encoding human homologs of MutL cause multiorgan cancer susceptibility. We have determined the crystal structure of a 40 kDa N-terminal fragment of E. coli MutL that retains all of the conserved residues in the MutL family. The structure of MutL is homologous to that of an ATPase-containing fragment of DNA gyrase. We have demonstrated that MutL binds and hydrolyzes ATP to ADP and Pi. Mutations in the MutL family that cause deficiencies in DNA mismatch repair and a predisposition to cancer mainly occur in the putative ATP-binding site. We provide evidence that the flexible, yet conserved, loops surrounding this ATP-binding site undergo conformational changes upon ATP hydrolysis thereby modulating interactions between MutL and other components of the repair machinery.

Selected figure(s)

Figure 4.
Figure 4. Structural Comparison of LN40, NgyrB, and Hsp90(a) Ribbon diagrams of NgyrB, LN40, and human Hsp90 (PDB accession number: 1YET). The four conserved ATP-binding motifs are highlighted in red.(b) Structural elements that form the ATP-binding site in NgyrB and LN40. Helices are represented as cylinders, strands as arrows. The four ATP-binding motifs are labeled in NgyrB. ADPnP, side chains that contributed to ADPnP binding in NgyrB, and their counterparts in LN40 are shown in ball-and-stick.(c) Orthogonal views of overlay of the Cα traces of LN40 and NgyrB. Residues at the N and C termini of NgyrB are omitted for clarity. The regions in NgyrB that are equivalent to the L2 and L3 loops in LN40 are labeled.(d) Structure-based sequence alignment of MutL and NgyrB. Identical sequences are outlined in red; conserved changed are outlined in yellow. The four ATP-binding motifs from human HSP90 are also included. The secondary structures of LN40 are shown above the sequence alignment.

Figure 5.
Figure 5. Ribbon Diagram of a Structurally Similar Domain in MutL, DNA Gyrase, and EF-G

The above figures are reprinted by permission from Cell Press: Cell (1998, 95, 541-552) copyright 1998.

Figures were selected by an automated process.