1ATG

AZOTOBACTER VINELANDII PERIPLASMIC MOLYBDATE-BINDING PROTEIN

Summary for 1ATG

• Entry DOI: 10.2210/pdb1atg/pdb
• Descriptor: PERIPLASMIC MOLYBDATE-BINDING PROTEIN, TUNGSTATE(VI)ION, ACETATE ION, ... (6 entities in total)
• Functional Keywords: molybdate, tungstate, binding protein, periplasm, abc transporter
• Biological source: Azotobacter vinelandii
• Total number of polymer chains: 1
• Total formula weight: 24917.81

Authors

Lawson, D.M.,Pau, R.N.,Williams, C.E.M.,Mitchenall, L.A. (deposition date: 1997-08-14, release date: 1998-10-14, Last modification date: 2024-02-07)

Primary citation

Lawson, D.M.,Williams, C.E.,Mitchenall, L.A.,Pau, R.N.
Ligand size is a major determinant of specificity in periplasmic oxyanion-binding proteins: the 1.2 A resolution crystal structure of Azotobacter vinelandii ModA.
Structure, 6:1529-1539, 1998

PubMed Abstract: . Periplasmic receptors constitute a diverse class of binding proteins that differ widely in size, sequence and ligand specificity. Nevertheless, almost all of them display a common beta/alpha folding motif and have similar tertiary structures consisting of two globular domains. The ligand is bound at the bottom of a deep cleft, which lies at the interface between these two domains. The oxyanion-binding proteins are notable in that they can discriminate between very similar ligands.

PubMed: 9862806
DOI: 10.1016/S0969-2126(98)00151-8

Experimental method

X-RAY DIFFRACTION (1.2 Å)