PDBsum entry 4x9r

Transferase/transferase inhibitor

PDB id: 4x9r

Contents

Protein chain

220 a.a.

Ligands

4L0-LEU-56A-SER-TPO-NH2

Waters ×189

PDB id:

4x9r

Name:

Transferase/transferase inhibitor

Title:

Plk-1 polo-box domain in complex with bioactive imidazolium-containing phosphopeptide macrocycle 3b

Structure:

Serine/threonine-protein kinase plk1. Chain: a. Fragment: polo-box domain residues 371-603. Synonym: polo-like kinase 1,plk-1,serine/threonine-protein kinase 13, stpk13. Engineered: yes. Phosphopeptide macrocycle 3b. Chain: b. Synonym: 1-(1-methylethyl)-1h-benzimidazole-2-sulfonic acid.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: plk1, plk. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Synthetic construct. Organism_taxid: 32630

Resolution:

1.40Å R-factor: 0.151 R-free: 0.179

Authors:

R.A.Grant,W.-J.Qian,M.B.Yaffe,T.R.Burke

Key ref:

W.J.Qian et al. (2015). Neighbor-directed histidine N (τ)-alkylation: A route to imidazolium-containing phosphopeptide macrocycles. Biopolymers, 104, 663-673. PubMed id: 26152807 DOI: 10.1002/bip.22698

Date:

11-Dec-14 Release date: 29-Jul-15

Protein chain

P53350  (PLK1_HUMAN) -  Serine/threonine-protein kinase PLK1 from Homo sapiens

Seq: 603 a.a.

Struc: 220 a.a.

Enzyme reactions

• Enzyme class: E.C.2.7.11.21 - polo 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/bip.22698

Biopolymers 104:663-673 (2015)

PubMed id: 26152807

Neighbor-directed histidine N (τ)-alkylation: A route to imidazolium-containing phosphopeptide macrocycles.

W.J.Qian, J.E.Park, R.Grant, C.C.Lai, J.A.Kelley, M.B.Yaffe, K.S.Lee, T.R.Burke.

ABSTRACT

Our recently discovered, selective, on-resin route to N(τ)-alkylated imidazolium-containing histidine residues affords new strategies for peptide mimetic design. In this, we demonstrate the use of this chemistry to prepare a series of macrocyclic phosphopeptides, in which imidazolium groups serve as ring-forming junctions. Interestingly, these cationic moieties subsequently serve to charge-mask the phosphoamino acid group that directed their formation. Neighbor-directed histidine N(τ)-alkylation opens the door to new families of phosphopeptidomimetics for use in a range of chemical biology contexts. © 2015 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 104: 663-673, 2015.