PDBsum entry 3hyj

Transcription regulator

PDB id: 3hyj

Contents

Protein chains

186 a.a. *

198 a.a. *

Ligands

GOL ×2

Metals

_NA

_CL ×2

Waters ×57

* Residue conservation analysis

PDB id:

3hyj

Name:

Transcription regulator

Title:

Crystal structure of the n-terminal laglidadg domain of duf199/whia

Structure:

Protein duf199/whia. Chain: a, d. Fragment: n-terminal domain, generated by proteolytic digestion of the full-length protein (unp residues 1 to 198). Engineered: yes

Source:

Thermotoga maritima. Organism_taxid: 2336. Gene: msb8, tm_1708. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.60Å R-factor: 0.201 R-free: 0.260

Authors:

B.K.Kaiser,M.C.Clifton,B.W.Shen,B.L.Stoddard

Key ref:

B.K.Kaiser et al. (2009). The structure of a bacterial DUF199/WhiA protein: domestication of an invasive endonuclease. Structure, 17, 1368-1376. PubMed id: 19836336

Date:

22-Jun-09 Release date: 01-Sep-09

Protein chain

Q9X234  (Q9X234_THEMA) -  Probable cell division protein WhiA from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)

Seq: 295 a.a.

Struc: 186 a.a.

Protein chain

Q9X234  (Q9X234_THEMA) -  Probable cell division protein WhiA from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)

Seq: 295 a.a.

Struc: 198 a.a.

Enzyme reactions

• Enzyme class: Chains A, D: E.C.?

Structure 17:1368-1376 (2009)

PubMed id: 19836336

The structure of a bacterial DUF199/WhiA protein: domestication of an invasive endonuclease.

B.K.Kaiser, M.C.Clifton, B.W.Shen, B.L.Stoddard.

ABSTRACT

Proteins of the DUF199 family, present in all Gram-positive bacteria and best characterized by the WhiA sporulation control factor in Streptomyces coelicolor, are thought to act as genetic regulators. The crystal structure of the DUF199/WhiA protein from Thermatoga maritima demonstrates that these proteins possess a bipartite structure, in which a degenerate N-terminal LAGLIDADG homing endonuclease (LHE) scaffold is tethered to a C-terminal helix-turn-helix (HTH) domain. The LHE domain has lost those residues critical for metal binding and catalysis, and also displays an extensively altered DNA-binding surface as compared with homing endonucleases. The HTH domain most closely resembles related regions of several bacterial sigma70 factors that bind the -35 regions of bacterial promoters. The structure illustrates how an invasive element might be transformed during evolution into a larger assemblage of protein folds that can participate in the regulation of a complex biological pathway.