PDBsum entry 4zki

Transferase

PDB id: 4zki

Contents

Protein chains

233 a.a.

209 a.a.

Ligands

ADP

PDB id:

4zki

Name:

Transferase

Title:

The crystal structure of histidine kinase yycg with adp

Structure:

Histidine kinase. Chain: a, b. Fragment: unp residues 370-624. Synonym: yycg. Engineered: yes

Source:

Lactobacillus plantarum jdm1. Organism_taxid: 644042. Strain: jdm1. Gene: hpk1, jdm1_0052. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

3.40Å R-factor: 0.203 R-free: 0.222

Authors:

Y.Cai

Key ref:

Y.Cai et al. (2017). Conformational dynamics of the essential sensor histidine kinase WalK. Acta Crystallogr D Struct Biol, 73, 793-803. PubMed id: 28994408

Date:

30-Apr-15 Release date: 04-May-16

Protein chain

A0A0M3KKX3  (A0A0M3KKX3_LACPJ) -  histidine kinase from Lactiplantibacillus plantarum (strain JDM1)

Seq: 193 a.a.

Struc: 233 a.a.

Protein chain

A0A0M3KKX3  (A0A0M3KKX3_LACPJ) -  histidine kinase from Lactiplantibacillus plantarum (strain JDM1)

Seq: 193 a.a.

Struc: 209 a.a.

Enzyme reactions

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

ATP + protein L-histidine = ADP (Bound ligand (Het Group name = ADP) corresponds exactly) + protein N-phospho-L-histidine

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

reference

Acta Crystallogr D Struct Biol 73:793-803 (2017)

PubMed id: 28994408

Conformational dynamics of the essential sensor histidine kinase WalK.

Y.Cai, M.Su, A.Ahmad, X.Hu, J.Sang, L.Kong, X.Chen, C.Wang, J.Shuai, A.Han.

ABSTRACT

Two-component systems (TCSs) are key elements in bacterial signal transduction in response to environmental stresses. TCSs generally consist of sensor histidine kinases (SKs) and their cognate response regulators (RRs). Many SKs exhibit autokinase, phosphoryltransferase and phosphatase activities, which regulate RR activity through a phosphorylation and dephosphorylation cycle. However, how SKs perform different enzymatic activities is poorly understood. Here, several crystal structures of the minimal catalytic region of WalK, an essential SK from Lactobacillus plantarum that shares 60% sequence identity with its homologue VicK from Streptococcus mutans, are presented. WalK adopts an asymmetrical closed structure in the presence of ATP or ADP, in which one of the CA domains is positioned close to the DHp domain, thus leading both the β- and γ-phosphates of ATP/ADP to form hydrogen bonds to the ℇ- but not the δ-nitrogen of the phosphorylatable histidine in the DHp domain. In addition, the DHp domain in the ATP/ADP-bound state has a 25.7° asymmetrical helical bending coordinated with the repositioning of the CA domain; these processes are mutually exclusive and alternate in response to helicity changes that are possibly regulated by upstream signals. In the absence of ATP or ADP, however, WalK adopts a completely symmetric open structure with its DHp domain centred between two outward-reaching CA domains. In summary, these structures of WalK reveal the intrinsic dynamic properties of an SK structure as a molecular basis for multifunctionality.