1spi
From Proteopedia
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CRYSTAL STRUCTURE OF SPINACH CHLOROPLAST FRUCTOSE-1,6-BISPHOSPHATASE AT 2.8 ANGSTROMS RESOLUTION
Overview
The three-dimensional structure of the spinach chloroplast, fructose-1,6-bisphosphatase (Fru-1,6-Pase) has been solved by the, molecular replacement method at 2.8 A resolution and refined to a, crystallographic R factor of 0.203. The enzyme is composed of four, monomers and displays pseudo D2 symmetry. Comparison with the allosteric, Fru-1,6-Pase from pig kidney shows orientationally displaced dimers within, the quaternary structure of the chloroplast enzyme. When the C1C2 dimers, of the two enzymes are superimposed, the C3C4 dimer of the chloroplast, enzyme is rotated 20 degrees and 5 degrees relative to the C3C4 dimer of, the R and T forms of the pig kidney enzyme, respectively. This new, quaternary structure, designated as S, may be described as a super-T form, and is outside of the pathway of the allosteric transition which occurs in, the pig kidney enzyme, which shows a 15 degrees rotation between T and R, forms. Chloroplast Fru-1,6-Pase, unlike the pig kidney enzyme, is, insensitive to allosteric transformation by AMP. Structural changes in the, AMP binding site involving mainly helices H1, H2, and H3 and the loop, between H1 and H2 at the dimer interface interfere with binding of the, phosphate of AMP. Finally, the location of cysteines residues provides a, basis for a preliminary discussion of the activation of the enzyme by, reduction of cysteines via the ferredoxin-thioredoxin f system; this, process is complementary to activation by pH changes, Mg2+ or Ca2+, Fru-1,6-P2, and possibly Fru-2,6-P2.
About this Structure
1SPI is a Single protein structure of sequence from Spinacia oleracea. Active as Fructose-bisphosphatase, with EC number 3.1.3.11 Full crystallographic information is available from OCA.
Reference
Crystal structure of spinach chloroplast fructose-1,6-bisphosphatase at 2.8 A resolution., Villeret V, Huang S, Zhang Y, Xue Y, Lipscomb WN, Biochemistry. 1995 Apr 4;34(13):4299-306. PMID:7703243
Page seeded by OCA on Wed Nov 21 02:32:54 2007
