PDBsum entry: 1zun

Transferase

PDB id: 1zun

Contents

Protein chains

204 a.a. *

394 a.a. *

Ligands

AGS

GDP

Metals

_MG

_NA

Waters ×87

* Residue conservation analysis

PDB id:

1zun

Name:

Transferase

Title:

Crystal structure of a gtp-regulated atp sulfurylase heterodimer from pseudomonas syringae

Structure:

Sulfate adenylyltransferase subunit 2. Chain: a. Synonym: sulfate adenylate transferase, sat, atp- sulfurylase small subunit, atp sulfurylase catalytic subunit (cysd). Engineered: yes. Sulfate adenylate transferase, subunit 1/adenylylsulfate kinase. Chain: b.

Source:

Pseudomonas syringae. Organism_taxid: 317. Gene: cysd. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693. Pseudomonas syringae pv. Tomato str. Dc3000. Organism_taxid: 223283. Gene: cysnc.

Biol. unit:

Dimer (from PQS)

Resolution:

2.70Å R-factor: 0.224 R-free: 0.276

Authors:

J.D.Mougous,D.H.Lee,S.C.Hubbard,M.W.Schelle,D.J.Vocadlo, J.M.Berger,C.R.Bertozzi

Key ref:

J.D.Mougous et al. (2006). Molecular basis for g protein control of the prokaryotic ATP sulfurylase. Mol Cell, 21, 109-122. PubMed id: 16387658 DOI: 10.1016/j.molcel.2005.10.034

Date:

31-May-05 Release date: 17-Jan-06

Protein chain

Q87WW0  (CYSD_PSESM) -  Sulfate adenylyltransferase subunit 2

Seq: 305 a.a.

Struc: 204 a.a.

Protein chain

Q87WW1  (Q87WW1_PSESM) -  Sulfate adenylate transferase, subunit 1/adenylylsulfate kinase

Seq: 632 a.a.

Struc: 394 a.a.

Enzyme reactions

• Enzyme class: Chain A: E.C.2.7.7.4 - Sulfate adenylyltransferase.
• Reaction: ATP + sulfate = diphosphate + adenylyl sulfate

ATP (Bound ligand (Het Group name = AGS) matches with 93.00% similarity) + sulfate = diphosphate + adenylyl sulfate

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

 Gene Ontology (GO) functional annotation 

• Biological process: metabolic process (2 terms)
• Biochemical function: nucleotide binding (8 terms)

reference

DOI no: 10.1016/j.molcel.2005.10.034

Mol Cell 21:109-122 (2006)

PubMed id: 16387658

Molecular basis for g protein control of the prokaryotic ATP sulfurylase.

J.D.Mougous, D.H.Lee, S.C.Hubbard, M.W.Schelle, D.J.Vocadlo, J.M.Berger, C.R.Bertozzi.

ABSTRACT

Sulfate assimilation is a critical component of both primary and secondary metabolism. An essential step in this pathway is the activation of sulfate through adenylation by the enzyme ATP sulfurylase (ATPS), forming adenosine 5'-phosphosulfate (APS). Proteobacterial ATPS overcomes this energetically unfavorable reaction by associating with a regulatory G protein, coupling the energy of GTP hydrolysis to APS formation. To discover the molecular basis of this unusual role for a G protein, we biochemically characterized and solved the X-ray crystal structure of a complex between Pseudomonas syringae ATPS (CysD) and its associated regulatory G protein (CysN). The structure of CysN*D shows the two proteins in tight association; however, the nucleotides bound to each subunit are spatially segregated. We provide evidence that conserved switch motifs in the G domain of CysN allosterically mediate interactions between the nucleotide binding sites. This structure suggests a molecular mechanism by which conserved G domain architecture is used to energetically link GTP turnover to the production of an essential metabolite.

Selected figure(s)

Figure 1.
Figure 1. Overview of Bacterial Sulfate Assimilation

Figure 2.
Figure 2. The APS Kinase Portion of the P. syringae CysNC Fusion Is Inactivated by Mutation of Conserved APS Binding Residues

The above figures are reprinted by permission from Cell Press: Mol Cell (2006, 21, 109-122) copyright 2006.

Figures were selected by the author.