The structure of Mg-ATPase nucleotide-binding domain at 1.6 Å resolution reveals a unique ATP-binding motif

The structure of the nucleotide‐binding domain of the Mg‐ATPase MgtA from Escherichia coli has been solved and refined to 1.6 Å resolution. The structure is made up of a six‐stranded β‐sheet and a bundle of three α‐helices, with the nucleotide‐binding site sandwiched in between. The MgtA nucleotide‐...

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Veröffentlicht in:	Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2009-11, Vol.65 (11), p.1181-1186
1. Verfasser:	Håkansson, Kjell O.
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphatases - chemistry Adenosine Triphosphatases - metabolism Adenosine Triphosphate - chemistry Adenosine Triphosphate - metabolism Amino Acid Sequence ATP binding Binding Sites Crystallography, X-Ray Escherichia coli - enzymology Escherichia coli Proteins - chemistry Escherichia coli Proteins - metabolism membrane proteins Membrane Transport Proteins - chemistry Membrane Transport Proteins - metabolism MgtA MgtB Models, Molecular Molecular Sequence Data P-type ATPases Protein Binding Protein Folding Protein Interaction Domains and Motifs Sequence Alignment Sequence Homology, Amino Acid
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