PDBsum entry 5c5e

Transcription

PDB id: 5c5e

Contents

Protein chains

284 a.a.

16 a.a.

20 a.a.

Ligands

52M ×2

Waters ×98

PDB id:

5c5e

Name:

Transcription

Title:

Structure of kaia dimer in complex with c-terminal kaic peptide at 2.8 a resolution

Structure:

Circadian clock protein kaia. Chain: a, b. Engineered: yes. Kaic c-terminal peptide. Chain: g, h. Engineered: yes

Source:

Synechococcus elongatus (strain pcc 7942). Organism_taxid: 1140. Strain: pcc 7942. Gene: kaia, synpcc7942_1218, see0009. Expressed in: escherichia coli. Expression_system_taxid: 511693. Synthetic: yes. Synthetic construct. Organism_taxid: 32630

Resolution:

2.82Å R-factor: 0.243 R-free: 0.303

Authors:

R.Pattanayek,M.Egli

Key ref:

R.Pattanayek and M.Egli (2015). Protein-Protein Interactions in the Cyanobacterial Circadian Clock: Structure of KaiA Dimer in Complex with C-Terminal KaiC Peptides at 2.8 Å Resolution. Biochemistry, 54, 4575-4578. PubMed id: 26200123 DOI: 10.1021/acs.biochem.5b00694

Date:

19-Jun-15 Release date: 05-Aug-15

Protein chains

Q79PF6  (KAIA_SYNE7) -  Circadian clock oscillator protein KaiA from Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805)

Seq: 284 a.a.

Struc: 284 a.a.

Protein chain

Q79PF4  (KAIC_SYNE7) -  Circadian clock oscillator protein KaiC from Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805)

Seq: 519 a.a.

Struc: 16 a.a.

Protein chain

Q79PF4  (KAIC_SYNE7) -  Circadian clock oscillator protein KaiC from Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805)

Seq: 519 a.a.

Struc: 20 a.a.

Enzyme reactions

• Enzyme class 1: Chains A, B: E.C.?
• Enzyme class 2: Chains G, H: 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⁺
• Enzyme class 3: Chains G, H: E.C.3.6.4.- - ?????

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

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

reference

DOI no: 10.1021/acs.biochem.5b00694

Biochemistry 54:4575-4578 (2015)

PubMed id: 26200123

Protein-Protein Interactions in the Cyanobacterial Circadian Clock: Structure of KaiA Dimer in Complex with C-Terminal KaiC Peptides at 2.8 Å Resolution.

R.Pattanayek, M.Egli.

ABSTRACT

In the cyanobacterial circadian clock, the KaiA, -B, and -C proteins with ATP constitute a post-translational oscillator. KaiA stimulates the KaiC autokinase, and KaiB antagonizes KaiA action. KaiA contacts the intrinsically disordered C-terminal regions of KaiC hexamer to promote phosphorylation across subunit interfaces. The crystal structure of KaiA dimer from Synechococcus elongatus with two KaiC C-terminal 20mer peptides bound reveals that the latter adopt an α-helical conformation and contact KaiA α-helical bundles via mostly hydrophobic interactions. This complex and the crystal structure of KaiC hexamer with truncated C-terminal tails can be fit into the electron microscopy (EM) density of the KaiA:KaiC complex. The hybrid model helps rationalize clock phenotypes of KaiA and KaiC mutants.