5LBD

Crystal structure of the N-domain of HMA6, a copper-transporting P-type ATPase

Summary for 5LBD

• Entry DOI: 10.2210/pdb5lbd/pdb
• Descriptor: Copper-transporting ATPase PAA1, chloroplastic, IODIDE ION, AMMONIUM ION, ... (6 entities in total)
• Functional Keywords: p-type atpase, copper transporter, chloroplast, inner membrane, hydrolase, membrane protein
• Biological source: Arabidopsis thaliana (Mouse-ear cress)
• Cellular location: Plastid, chloroplast membrane ; Multi- pass membrane protein : Q9SZC9
• Total number of polymer chains: 2
• Total formula weight: 29042.73

Authors

Mayerhofer, H.,Ravaud, S.,Pebay-Peyroula, E. (deposition date: 2016-06-15, release date: 2017-08-02, Last modification date: 2024-10-16)

Primary citation

Mayerhofer, H.,Sautron, E.,Rolland, N.,Catty, P.,Seigneurin-Berny, D.,Pebay-Peyroula, E.,Ravaud, S.
Structural Insights into the Nucleotide-Binding Domains of the P1B-type ATPases HMA6 and HMA8 from Arabidopsis thaliana.
PLoS ONE, 11:e0165666-e0165666, 2016

PubMed Abstract: Copper is a crucial ion in cells, but needs to be closely controlled due to its toxic potential and ability to catalyse the formation of radicals. In chloroplasts, an important step for the proper functioning of the photosynthetic electron transfer chain is the delivery of copper to plastocyanin in the thylakoid lumen. The main route for copper transport to the thylakoid lumen is driven by two PIB-type ATPases, Heavy Metal ATPase 6 (HMA6) and HMA8, located in the inner membrane of the chloroplast envelope and in the thylakoid membrane, respectively. Here, the crystal structures of the nucleotide binding domain of HMA6 and HMA8 from Arabidopsis thaliana are reported at 1.5Å and 1.75Å resolution, respectively, providing the first structural information on plants Cu+-ATPases. The structures reveal a compact domain, with two short helices on both sides of a twisted beta-sheet. A double mutant, aiding in the crystallization, provides a new crystal contact, but also avoids an internal clash highlighting the benefits of construct modifications. Finally, the histidine in the HP motif of the isolated domains, unable to bind ATP, shows a side chain conformation distinct from nucleotide bound structures.

PubMed: 27802305
DOI: 10.1371/journal.pone.0165666

Experimental method

X-RAY DIFFRACTION (1.5 Å)