PDBsum entry 2jex

Transcription

PDB id

2jex

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Contents

			Protein chain

					197 a.a. *

			Waters ×115

* Residue conservation analysis

PDB id:

2jex

Links

Name:

Transcription

Title:

Transcription activator structure reveals redox control of a replication initiation reaction

Structure:

Regulatory protein e2. Chain: a. Fragment: n-terminal trans-activation domain (tad), residues 1-209. Engineered: yes. Mutation: yes

Source:

Bovine papillomavirus type 1. Organism_taxid: 10559. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

2.35Å

R-factor:

0.211

R-free:

0.241

Authors:

C.M.Sanders,D.Sizov,P.R.Seavers,M.Ortiz-Lombardia,A.A.Antson

Key ref:

C.M.Sanders et al. (2007). Transcription activator structure reveals redox control of a replication initiation reaction. Nucleic Acids Res, 35, 3504-3515. PubMed id: 17478495

Date:

24-Jan-07

Release date:

15-May-07

PROCHECK

	Headers

	References

Protein chain

P03122 (VE2_BPV1) - Regulatory protein E2 from Bovine papillomavirus type 1

Seq: Struc:					410 a.a. 197 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

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

	Nucleic Acids Res 35:3504-3515 (2007)
PubMed id: 17478495

Transcription activator structure reveals redox control of a replication initiation reaction.
C.M.Sanders, D.Sizov, P.R.Seavers, M.Ortiz-Lombardía, A.A.Antson.

ABSTRACT

Redox changes are one of the factors that influence cell-cycle progression and that control the processes of cellular proliferation, differentiation, senescence and apoptosis. Proteins regulated through redox-sensitive cysteines have been characterized but specific 'sulphydryl switches' in replication proteins remain to be identified. In bovine papillomavirus type-1, DNA replication begins when the viral transcription factor E2 recruits the viral initiator protein E1 to the origin of DNA replication (ori). Here we show that a novel dimerization interface in the E2 transcription activation domain is stabilized by a disulphide bond. Oxidative cross-linking via Cys57 sequesters the interaction surface between E1 and E2, preventing pre-initiation and replication initiation complex formation. Our data demonstrate that as well as a mechanism for regulating DNA binding, redox reactions can control replication by modulating the tertiary structure of critical protein factors using a specific redox sensor.

Literature references that cite this PDB file's key reference

PubMed id

Reference

19039000

D.Sela, and J.Shlomai (2009).
Regulation of UMSBP activities through redox-sensitive protein domains.

Nucleic Acids Res, 37, 279-288.

19521517

S.Aras, G.Singh, K.Johnston, T.Foster, and A.Aiyar (2009).
Zinc coordination is required for and regulates transcription activation by Epstein-Barr nuclear antigen 1.

PLoS Pathog, 5, e1000469.

18337573

E.E.Hernandez-Ramon, J.E.Burns, W.Zhang, H.F.Walker, S.Allen, A.A.Antson, and N.J.Maitland (2008).
Dimerization of the human papillomavirus type 16 E2 N terminus results in DNA looping within the upstream regulatory region.

J Virol, 82, 4853-4861.

18495759

J.Cardenas-Mora, J.E.Spindler, M.K.Jang, and A.A.McBride (2008).
Dimerization of the papillomavirus E2 protein is required for efficient mitotic chromosome association and Brd4 binding.

J Virol, 82, 7298-7305.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.