PDBsum entry 2zoq

Transferase

PDB id: 2zoq

Contents

Protein chain

352 a.a. *

Ligands

SO4 ×2

5ID ×2

Metals

_NA ×2

Waters ×314

* Residue conservation analysis

PDB id:

2zoq

Name:

Transferase

Title:

Structural dissection of human mitogen-activated kinase erk1

Structure:

Mitogen-activated protein kinase 3. Chain: a, b. Synonym: extracellular signal-regulated kinase 1, erk-1, insulin- stimulated map2 kinase, map kinase 1, mapk 1, p44-erk1, ert2, p44- mapk, microtubule-associated protein 2 kinase. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: mapk3, erk1, prkm3. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.39Å R-factor: 0.249 R-free: 0.267

Authors:

T.Kinoshita,T.Tada,S.Nakae,I.Yoshida

Key ref:

T.Kinoshita et al. (2008). Crystal structure of human mono-phosphorylated ERK1 at Tyr204. Biochem Biophys Res Commun, 377, 1123-1127. PubMed id: 18983981

Date:

01-Jun-08 Release date: 07-Apr-09

Protein chains

P27361  (MK03_HUMAN) -  Mitogen-activated protein kinase 3 from Homo sapiens

Seq: 379 a.a.

Struc: 352 a.a.

Enzyme reactions

• Enzyme class: E.C.2.7.11.24 - mitogen-activated 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⁺

L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] (Bound ligand (Het Group name = 5ID) matches with 62.07% similarity) + ADP + H(+)

L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] (Bound ligand (Het Group name = 5ID) matches with 62.07% similarity) + ADP + H(+)

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

reference

Biochem Biophys Res Commun 377:1123-1127 (2008)

PubMed id: 18983981

Crystal structure of human mono-phosphorylated ERK1 at Tyr204.

T.Kinoshita, I.Yoshida, S.Nakae, K.Okita, M.Gouda, M.Matsubara, K.Yokota, H.Ishiguro, T.Tada.

ABSTRACT

Extracellular signal-regulated kinase (ERK) is a member of the MAP kinase family, and can regulate several cellular responses. The isoforms ERK1 and ERK2 have markedly similar amino acid sequences, but exhibit distinctive physiological functions. As well as ERK2, ERK1 was auto- and mono-phosphorylated at Tyr204 in the activation loop during Escherichia coli production, resulting in basal level activity, approximately 500-fold less compared with fully-active ERK1 dual-phosphorylated at Thr202 and Tyr204. Crystal structure demonstrated that the mono-phosphorylated ERK1 kinase possessed a novel conformation distinguishable from the un-phosphorylated (inactive) and the dual-phosphorylated (full-active) forms. The characteristic structural features in both the C-helix and the activation loop likely contribute to the basal activity of the mono-phosphorylated ERK1. The structural dissection of ERK1 compared to ERK2 suggests that the structural differences in the D-motif binding site and in the backside binding site are putative targets for development of selective ERK1/ERK2 inhibitors.