PDBsum entry 5cb8

Transferase

PDB id: 5cb8

Contents

Protein chains

174 a.a.

Ligands

ADX ×2

SO4 ×4

ACT ×2

Waters ×557

PDB id:

5cb8

Name:

Transferase

Title:

Crystal structure of adenosine-5'-phosphosulfate kinase in complex with aps and sulfate

Structure:

Probable adenylyl-sulfate kinase. Chain: a, b. Synonym: aps kinase,atp adenosine-5'-phosphosulfate 3'- phosphotransferase,adenosine-5'-phosphosulfate kinase. Engineered: yes

Source:

Synechocystis sp. (Strain pcc 6803 / kazusa). Organism_taxid: 1111708. Strain: pcc 6803 / kazusa. Gene: cysc, slr0676. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

1.88Å R-factor: 0.156 R-free: 0.176

Authors:

J.Herrmann,J.M.Jez

Key ref:

J.Herrmann et al. (2015). Recapitulating the Structural Evolution of Redox Regulation in Adenosine 5'-Phosphosulfate Kinase from Cyanobacteria to Plants. J Biol Chem, 290, 24705-24714. PubMed id: 26294763 DOI: 10.1074/jbc.M115.679514

Date:

30-Jun-15 Release date: 02-Sep-15

Protein chains

P72940  (CYSC_SYNY3) -  Probable adenylyl-sulfate kinase from Synechocystis sp. (strain PCC 6803 / Kazusa)

Seq: 177 a.a.

Struc: 174 a.a.

Enzyme reactions

• Enzyme class: E.C.2.7.1.25 - adenylyl-sulfate kinase.
• Reaction: adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H⁺

adenosine 5'-phosphosulfate (Bound ligand (Het Group name = ADX) corresponds exactly) + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)

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

reference

DOI no: 10.1074/jbc.M115.679514

J Biol Chem 290:24705-24714 (2015)

PubMed id: 26294763

Recapitulating the Structural Evolution of Redox Regulation in Adenosine 5'-Phosphosulfate Kinase from Cyanobacteria to Plants.

J.Herrmann, D.Nathin, S.G.Lee, T.Sun, J.M.Jez.

ABSTRACT

In plants, adenosine 5'-phosphosulfate (APS) kinase (APSK) is required for reproductive viability and the production of 3'-phosphoadenosine 5'-phosphosulfate (PAPS) as a sulfur donor in specialized metabolism. Previous studies of the APSK from Arabidopsis thaliana (AtAPSK) identified a regulatory disulfide bond formed between the N-terminal domain (NTD) and a cysteine on the core scaffold. This thiol switch is unique to mosses, gymnosperms, and angiosperms. To understand the structural evolution of redox control of APSK, we investigated the redox-insensitive APSK from the cyanobacterium Synechocystis sp. PCC 6803 (SynAPSK). Crystallographic analysis of SynAPSK in complex with either APS and a non-hydrolyzable ATP analog or APS and sulfate revealed the overall structure of the enzyme, which lacks the NTD found in homologs from mosses and plants. A series of engineered SynAPSK variants reconstructed the structural evolution of the plant APSK. Biochemical analyses of SynAPSK, SynAPSK H23C mutant, SynAPSK fused to the AtAPSK NTD, and the fusion protein with the H23C mutation showed that the addition of the NTD and cysteines recapitulated thiol-based regulation. These results reveal the molecular basis for structural changes leading to the evolution of redox control of APSK in the green lineage from cyanobacteria to plants.