PDBsum entry 3a0r

Transferase

PDB id: 3a0r

Contents

Protein chains

334 a.a. *

116 a.a. *

Metals

_HG

* Residue conservation analysis

PDB id:

3a0r

Name:

Transferase

Title:

Crystal structure of histidine kinase thka (tm1359) in complex with response regulator protein trra (tm1360)

Structure:

Sensor protein. Chain: a. Fragment: pas, catalytic domain, dhp domain. Synonym: histidine kinase thka. Engineered: yes. Response regulator. Chain: b. Synonym: trra. Engineered: yes.

Source:

Thermotoga maritima. Organism_taxid: 2336. Gene: tm_1359. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Gene: tm_1360.

Resolution:

3.80Å R-factor: 0.351 R-free: 0.371

Authors:

S.Yamada,H.Sugimoto,M.Kobayashi,A.Ohno,H.Nakamura,Y.Shiro

Key ref:

S.Yamada et al. (2009). Structure of PAS-linked histidine kinase and the response regulator complex. Structure, 17, 1333-1344. PubMed id: 19836334 DOI: 10.1016/j.str.2009.07.016

Date:

24-Mar-09 Release date: 20-Oct-09

Protein chain

Q9X180  (Q9X180_THEMA) -  histidine kinase from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)

Seq: 755 a.a.

Struc: 334 a.a.

Protein chain

Q9X181  (Q9X181_THEMA) -  Response regulator from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)

Seq: 116 a.a.

Struc: 116 a.a.*

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

Enzyme reactions

• Enzyme class: Chain A: E.C.2.7.13.3 - histidine kinase.
• Reaction: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine

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

reference

DOI no: 10.1016/j.str.2009.07.016

Structure 17:1333-1344 (2009)

PubMed id: 19836334

Structure of PAS-linked histidine kinase and the response regulator complex.

S.Yamada, H.Sugimoto, M.Kobayashi, A.Ohno, H.Nakamura, Y.Shiro.

ABSTRACT

We determined the structure of the complex of the sensory histidine kinase (HK) and its cognate response regulator (RR) in the two-component signal transduction system of Thermotoga maritima. This was accomplished by fitting the high-resolution structures of the isolated HK domains and the RR onto the electron density map (3.8 A resolution) of the HK/RR complex crystal. Based on the structural information, we evaluated the roles of both interdomain and intermolecular interactions in the signal transduction of the cytosolic PAS-linked HK and RR system, in particular the O(2)-sensor FixL/FixJ system. The PAS-sensor domain of HK interacts with the catalytic domain of the same polypeptide chain by creating an interdomain beta sheet. The interaction site between HK and RR, which was confirmed by NMR, is suitable for the intermolecular transfer reaction of the phosphoryl group, indicating that the observed interaction is important for the phosphatase activity of HK that dephosphorylates phospho-RR.

Selected figure(s)

Figure 1.
Figure 1. Structural Comparison of the PAS Domain of ThkA and the PAS-Sensor Domain of FixL
(A) Structure of the PAS domain of ThkA.
(B) In the FixL PAS domain, the structures of the oxy (red) and deoxy (gray) forms are superimposed. The heme in FixL is shown as a stick model.

Figure 4.
Figure 4. Construction of the Structure of the ThkA/TrrA Complex
(A) Electron density (final 2F[o] − F[c] map) of the 2:2 complex at 3.8 Å resolution. Red spheres are the anomalous differences Fourier maps (3.5 σ) of either Hg or Se atoms obtained from the crystal of Hg-SeMet-ThkA (F486M,F489M,H546M)/SeMet-TrrA(D52M,L89M) (see Table S5).
(B) The map (A) is viewed along a two-fold axis and the map is represented as a grid.
(C) The overall ThkA/TrrA complex in the 2:2 dimer. The view is the same as in (A).
(D) The structure viewed along a two-fold axis.
(E–H) Qualities of the fitting into the map (2F[o] − F[c] map contoured at 1 σ) for the PAS domain of ThkA (E), DHp of ThkA (F), CA of ThkA (G), and TrrA (H).

The above figures are reprinted by permission from Cell Press: Structure (2009, 17, 1333-1344) copyright 2009.

Figures were selected by an automated process.