Glutamine PRPP amidotransferase structure [1]

PDB	scop	BSM	RELI Base	Header	¹
1ao0	-	1ao0	-	Glutamine PRPP amidotransferase (complex with GMP, ADP and Mg2+); Bacillus subtilis (recombinant form expressed in Escherichia coli)	-

a

b	d
c	e

¹ Macromolecular Structures abstract. Full text is available to BioMedNet Members

1. Ribbon representation of the Bacillus subtilis Glutamine PRPP amidotransferase structure (PDB code 1AO0). Colour­codes: chain A = yellow; chain B = light blue; chain C = green; chain D = red. Bound ADP and GMP are not shown.

   b-e: orientation as a, rotated -90° around y axis.

2. The [Fe₄S₄] cluster and its ligand residues.
3. As a, chain B, complex with ADP (left) and GMP (right). Colour­codes: glutamine domain (residues 1-226) = violet; transferase domain (residues 237-459) = blue; linker peptide (residues 226-237) = cyan.
4. As c, glutamine domain. N­terminus (residues 1-2) = white; C­terminus (residues 226-231) = green.
5. As c, transferase domain. N­terminus (residues 231-237) = white; allosteric (A) site (residues 303-331) = yellow; catalytic (C) site (residues 340-363) = cyan; C­terminus (residues 442-459) = green. ADP binds to the A site and GMP to the C site.

1. Chen, S., Tomchick, D.R., Wolle, D., Hu, P., Smith, J.L., Switzer, R.L. and Zalkin, H. (1997) Mechanism of the synergistic end­product regulation of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase by nucleotides. Biochemistry 36, 10718-10726.
2. Kraulis, P.J. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structure. J. Appl. Crystallogr. 24, 946-950.

Bibliography on structural studies of glutamine PRPP amidotransferase