PDBsum entry 4bt0

Transcription

PDB id: 4bt0

Contents

Protein chains

73 a.a.

173 a.a.

Ligands

ADP ×2

PDB id:

4bt0

Name:

Transcription

Title:

Mub is an aaaplus atpase that forms helical filaments to control target selection for DNA transposition

Structure:

Transcriptional regulator. Chain: a. Fragment: aaaplus domain, residues 312-384. Synonym: mub aaaplus atpase. Engineered: yes. Transcriptional regulator. Chain: b. Fragment: aaaplus domain, residues 137-309. Synonym: mub aaaplus atpase.

Source:

Enterobacteria phage mu. Organism_taxid: 10677. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_taxid: 562

Authors:

N.Mizuno,M.Dramicanin,M.Mizuuchi,J.Adam,Y.Wang,Y.W.Han,W.Yang, A.C.Steven,K.Mizuuchi,S.Ramon-Maiques

Key ref:

N.Mizuno et al. (2013). MuB is an AAA+ ATPase that forms helical filaments to control target selection for DNA transposition. Proc Natl Acad Sci U S A, 110, E2441. PubMed id: 23776210 DOI: 10.1073/pnas.1309499110

Date:

12-Jun-13 Release date: 03-Jul-13

Protein chain

O67198  (O67198_AQUAE) -  Transcriptional regulator (NtrC family) from Aquifex aeolicus (strain VF5)

Seq: 439 a.a.

Struc: 73 a.a.

Protein chain

O67198  (O67198_AQUAE) -  Transcriptional regulator (NtrC family) from Aquifex aeolicus (strain VF5)

Seq: 439 a.a.

Struc: 173 a.a.

Enzyme reactions

• Enzyme class: Chains A, B: E.C.?

DOI no: 10.1073/pnas.1309499110

Proc Natl Acad Sci U S A 110:E2441 (2013)

PubMed id: 23776210

MuB is an AAA+ ATPase that forms helical filaments to control target selection for DNA transposition.

N.Mizuno, M.Dramićanin, M.Mizuuchi, J.Adam, Y.Wang, Y.W.Han, W.Yang, A.C.Steven, K.Mizuuchi, S.Ramón-Maiques.

ABSTRACT

MuB is an ATP-dependent nonspecific DNA-binding protein that regulates the activity of the MuA transposase and captures target DNA for transposition. Mechanistic understanding of MuB function has previously been hindered by MuB's poor solubility. Here we combine bioinformatic, mutagenic, biochemical, and electron microscopic analyses to unmask the structure and function of MuB. We demonstrate that MuB is an ATPase associated with diverse cellular activities (AAA+ ATPase) and forms ATP-dependent filaments with or without DNA. We also identify critical residues for MuB's ATPase, DNA binding, protein polymerization, and MuA interaction activities. Using single-particle electron microscopy, we show that MuB assembles into a helical filament, which binds the DNA in the axial channel. The helical parameters of the MuB filament do not match those of the coated DNA. Despite this protein-DNA symmetry mismatch, MuB does not deform the DNA duplex. These findings, together with the influence of MuB filament size on strand-transfer efficiency, lead to a model in which MuB-imposed symmetry transiently deforms the DNA at the boundary of the MuB filament and results in a bent DNA favored by MuA for transposition.