PDBsum entry 2wiu

Transferase/transcription

PDB id: 2wiu

Contents

Protein chains

431 a.a. *

71 a.a. *

401 a.a. *

71 a.a. *

Metals

_CL ×10

_HG ×7

Waters ×278

* Residue conservation analysis

PDB id:

2wiu

Name:

Transferase/transcription

Title:

Mercury-modified bacterial persistence regulator hipba

Structure:

Protein hipa. Chain: a, c. Synonym: protein kinase component of persistence regulator hipa. Engineered: yes. Hth-type transcriptional regulator hipb. Chain: b, d. Synonym: DNA-inding component of persistence regulator hipba. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 562. Strain: dh5alpha. Expressed in: escherichia coli. Expression_system_taxid: 469008. Other_details: invitrogen dh5alpha cells. Other_details: invitrogen dh5alpha

Resolution:

2.35Å R-factor: 0.218 R-free: 0.264

Authors:

A.Evdokimov,I.Voznesensky,K.Fennell,M.Anderson,J.F.Smith,D.A.Fisher

Key ref:

A.Evdokimov et al. (2009). New kinase regulation mechanism found in HipBA: a bacterial persistence switch. Acta Crystallogr D Biol Crystallogr, 65, 875-879. PubMed id: 19622872 DOI: 10.1107/S0907444909018800

Date:

17-May-09 Release date: 28-Jul-09

Protein chain

P23874  (HIPA_ECOLI) -  Serine/threonine-protein kinase toxin HipA from Escherichia coli (strain K12)

Seq: 440 a.a.

Struc: 431 a.a.

Protein chain

P23873  (HIPB_ECOLI) -  Antitoxin HipB from Escherichia coli (strain K12)

Seq: 88 a.a.

Struc: 71 a.a.*

Protein chain

P23874  (HIPA_ECOLI) -  Serine/threonine-protein kinase toxin HipA from Escherichia coli (strain K12)

Seq: 440 a.a.

Struc: 401 a.a.

Protein chain

P23873  (HIPB_ECOLI) -  Antitoxin HipB from Escherichia coli (strain K12)

Seq: 88 a.a.

Struc: 71 a.a.*

* PDB and UniProt seqs differ at 7 residue positions (black crosses)

Enzyme reactions

• Enzyme class: Chains A, C: E.C.2.7.11.1 - non-specific serine/threonine protein kinase.
• Reaction:
  1. L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H⁺
  2. L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H⁺

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

reference

DOI no: 10.1107/S0907444909018800

Acta Crystallogr D Biol Crystallogr 65:875-879 (2009)

PubMed id: 19622872

New kinase regulation mechanism found in HipBA: a bacterial persistence switch.

A.Evdokimov, I.Voznesensky, K.Fennell, M.Anderson, J.F.Smith, D.A.Fisher.

ABSTRACT

Bacterial persistence is the ability of individual cells to randomly enter a period of dormancy during which the cells are protected against antibiotics. In Escherichia coli, persistence is regulated by the activity of a protein kinase HipA and its DNA-binding partner HipB, which is a strong inhibitor of both HipA activity and hip operon transcription. The crystal structure of the HipBA complex was solved by application of the SAD technique to a mercury derivative. In this article, the fortuitous and interesting effect of mercury soaks on the native HipBA crystals is discussed as well as the intriguing tryptophan-binding pocket found on the HipA surface. A HipA-regulation model is also proposed that is consistent with the available structural and biochemical data.

Selected figure(s)

Figure 3.
Figure 3 The tryptophan-binding pocket: the C-terminus of HipB is shown as a gray ball-and-stick model. HipA residues are colored blue (C-terminal domain) and green (N-terminal domain). Hydrogen bonds are represented by light blue dashed lines.

The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2009, 65, 875-879) copyright 2009.

Figure was selected by an automated process.