PDBsum entry 4zvc

Signaling protein

PDB id: 4zvc

Contents

Protein chains

116 a.a.

Ligands

BEZ

Waters ×255

PDB id:

4zvc

Name:

Signaling protein

Title:

Crystal structure of mid domain of the e. Coli dosc - form i

Structure:

Diguanylate cyclase dosc. Chain: a, b. Fragment: unp residues 173-298. Synonym: dgc,direct oxygen-sensing cyclase. Engineered: yes

Source:

Escherichia coli k-12. Organism_taxid: 83333. Gene: dosc, yddv, b1490, jw5241. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.50Å R-factor: 0.150 R-free: 0.189

Authors:

M.Tarnawski,T.R.M.Barends,I.Schlichting

Key ref:

M.Tarnawski et al. (2015). Structural analysis of an oxygen-regulated diguanylate cyclase. Acta Crystallogr D Biol Crystallogr, 71, 2158-2177. PubMed id: 26527135 DOI: 10.1107/S139900471501545X

Date:

18-May-15 Release date: 11-Nov-15

Protein chains

P0AA89  (DOSC_ECOLI) -  Diguanylate cyclase DosC from Escherichia coli (strain K12)

Seq: 460 a.a.

Struc: 116 a.a.

Enzyme reactions

• Enzyme class: E.C.2.7.7.65 - diguanylate cyclase.
• Reaction: 2 GTP = 3',3'-c-di-GMP + 2 diphosphate
• Cofactor: Mg(2+); Mn(2+)

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

Added reference

DOI no: 10.1107/S139900471501545X

Acta Crystallogr D Biol Crystallogr 71:2158-2177 (2015)

PubMed id: 26527135

Structural analysis of an oxygen-regulated diguanylate cyclase.

M.Tarnawski, T.R.Barends, I.Schlichting.

ABSTRACT

Cyclic di-GMP is a bacterial second messenger that is involved in switching between motile and sessile lifestyles. Given the medical importance of biofilm formation, there has been increasing interest in understanding the synthesis and degradation of cyclic di-GMPs and their regulation in various bacterial pathogens. Environmental cues are detected by sensing domains coupled to GGDEF and EAL or HD-GYP domains that have diguanylate cyclase and phosphodiesterase activities, respectively, producing and degrading cyclic di-GMP. The Escherichia coli protein DosC (also known as YddV) consists of an oxygen-sensing domain belonging to the class of globin sensors that is coupled to a C-terminal GGDEF domain via a previously uncharacterized middle domain. DosC is one of the most strongly expressed GGDEF proteins in E. coli, but to date structural information on this and related proteins is scarce. Here, the high-resolution structural characterization of the oxygen-sensing globin domain, the middle domain and the catalytic GGDEF domain in apo and substrate-bound forms is described. The structural changes between the iron(III) and iron(II) forms of the sensor globin domain suggest a mechanism for oxygen-dependent regulation. The structural information on the individual domains is combined into a model of the dimeric DosC holoprotein. These findings have direct implications for the oxygen-dependent regulation of the activity of the cyclase domain.