3GWI

Crystal Structure of Mg-ATPase Nucleotide binding domain

Summary for 3GWI

• Entry DOI: 10.2210/pdb3gwi/pdb
• Descriptor: Magnesium-transporting ATPase, P-type 1, SULFATE ION (3 entities in total)
• Functional Keywords: p-type atpase, nucleotide binding, atp binding, mgta, membrane protein, cell inner membrane, cell membrane, hydrolase, magnesium, metal-binding, phosphoprotein, transmembrane
• Biological source: Escherichia coli
• Cellular location: Cell inner membrane ; Multi-pass membrane protein : P0ABB8
• Total number of polymer chains: 1
• Total formula weight: 19746.21

Authors

Hakansson, K.O. (deposition date: 2009-04-01, release date: 2009-12-15, Last modification date: 2024-03-20)

Primary citation

Hakansson, K.O.
The structure of Mg-ATPase nucleotide-binding domain at 1.6 A resolution reveals a unique ATP-binding motif
Acta Crystallogr.,Sect.D, 65:1181-1186, 2009

PubMed Abstract: The structure of the nucleotide-binding domain of the Mg-ATPase MgtA from Escherichia coli has been solved and refined to 1.6 A resolution. The structure is made up of a six-stranded beta-sheet and a bundle of three alpha-helices, with the nucleotide-binding site sandwiched in between. The MgtA nucleotide-binding domain is shorter and more compact compared with that of the related Ca-ATPase and lacks one of the beta-strands at the edge of the beta-sheet. The ATP-binding pocket is surrounded by three sequence and structural motifs known from other P-type ATPases and a fourth unique motif that is found only in Mg-ATPases. This motif consists of a short polypeptide stretch running very close to the ATP-binding site, while in Ca-ATPase the binding site is more open, with the corresponding polypeptide segment folded away from the active site.

PubMed: 19923713
DOI: 10.1107/S090744490903306X

Experimental method

X-RAY DIFFRACTION (1.6 Å)