PDBsum entry 4x3f

Transferase

PDB id: 4x3f

Contents

Protein chains

277 a.a.

Waters ×10

PDB id:

4x3f

Name:

Transferase

Title:

Crystal structure of the intracellular domain of the m. Tuberculosis ser/thr kinase pkna

Structure:

Serine/threonine-protein kinase pkna. Chain: a. Engineered: yes. Serine/threonine-protein kinase pkna. Chain: b. Engineered: yes. Serine/threonine-protein kinase pkna. Chain: c. Engineered: yes

Source:

Mycobacterium tuberculosis. Organism_taxid: 83332. Strain: atcc 25618 / h37rv. Gene: pkna, rv0015c, mtcy10h4.15c. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Expression_system_taxid: 469008

Resolution:

2.90Å R-factor: 0.220 R-free: 0.243

Authors:

T.Wagner,A.Wehenkel,P.M.Alzari,M.Bellinzoni

Key ref:

T.Wagner et al. (2015). The crystal structure of the catalytic domain of the ser/thr kinase PknA from M. tuberculosis shows an Src-like autoinhibited conformation. Proteins, 83, 982-988. PubMed id: 25586004 DOI: 10.1002/prot.24754

Date:

28-Nov-14 Release date: 21-Jan-15

Protein chains

P9WI83  (PKNA_MYCTU) -  Serine/threonine-protein kinase PknA from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

Seq: 431 a.a.

Struc: 277 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Enzyme reactions

• Enzyme class: 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: 10.1002/prot.24754

Proteins 83:982-988 (2015)

PubMed id: 25586004

The crystal structure of the catalytic domain of the ser/thr kinase PknA from M. tuberculosis shows an Src-like autoinhibited conformation.

T.Wagner, M.Alexandre, R.Duran, N.Barilone, A.Wehenkel, P.M.Alzari, M.Bellinzoni.

ABSTRACT

Signal transduction mediated by Ser/Thr phosphorylation in Mycobacterium tuberculosis has been intensively studied in the last years, as its genome harbors eleven genes coding for eukaryotic-like Ser/Thr kinases. Here we describe the crystal structure and the autophosphorylation sites of the catalytic domain of PknA, one of two protein kinases essential for pathogen's survival. The structure of the ligand-free kinase domain shows an auto-inhibited conformation similar to that observed in human Tyr kinases of the Src-family. These results reinforce the high conservation of structural hallmarks and regulation mechanisms between prokaryotic and eukaryotic protein kinases. Proteins 2015; 83:982-988. © 2015 Wiley Periodicals, Inc.