PDBsum entry 1bur

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Lyase PDB id
Protein chains
464 a.a.
123 a.a.
CAP ×4
_MG ×4
Waters ×1875

References listed in PDB file
Key reference
Title Orderly disposition of heterogeneous small subunits in d-Ribulose-1,5-Bisphosphate carboxylase/oxygenase from spinach.
Authors N.Shibata, T.Inoue, K.Fukuhara, Y.Nagara, R.Kitagawa, S.Harada, N.Kasai, K.Uemura, K.Kato, A.Yokota, Y.Kai.
Ref. J Biol Chem, 1996, 271, 26449-26452. [DOI no: 10.1074/jbc.271.43.26449]
PubMed id 8900108
Note In the PDB file this reference is annotated as "TO BE PUBLISHED". The citation details given above were identified by an automated search of PubMed on title and author names, giving a percentage match of 92%.
We determined the crystal structure of spinach ribulose-1, 5-bisphosphate carboxylase/oxygenase (Rubisco) by x-ray diffraction at 1.8-A resolution and found that the enzyme contained two kinds of S, SI and SII, present in equal number and disposed in an orderly way within the Rubisco holoenzyme. The electron density maps suggested that leucine was at residue 56 in SI, although histidine was at that position in SII. There were other residue differences. Thus, spinach Rubisco has a L8SI4SII4 subunit structure. The orderly disposition of the heterogeneous small subunits in the Rubisco holoenzyme provides accounts of a multigene family of S in plants.
Figure 2.
Fig. 2. Two-dimensional gel electrophoresis of purified spinach Rubisco. LSU and SSU indicate the L and S peptides, respectively. The stained gel between pI 5.88 and 6.60 is shown in the figure.
Figure 3.
Fig. 3. Schematic drawing of the L[8]SI[4]SII[4] structure. The SI and SII subunits are shown as green and yellow stick models, respectively. The white dots show the C atoms of the eight large subunits. There are three 2-fold axes in the spinach Rubisco molecule; one of them corresponds to a crystallographic axis (red), and the others are noncrystallographic axes (white). This drawing was prepared using MidasPlus (30).
The above figures are reprinted by permission from the ASBMB: J Biol Chem (1996, 271, 26449-26452) copyright 1996.
Secondary reference #1
Title Crystallographic analysis of ribulose 1,5-Bisphosphate carboxylase from spinach at 2.4 a resolution. Subunit interactions and active site.
Authors S.Knight, I.Andersson, C.I.Brändén.
Ref. J Mol Biol, 1990, 215, 113-160.
PubMed id 2118958
Secondary reference #2
Title Large single crystals of spinach 1,5-Bisphosphate carboxylase/oxygenase suitable for x-Ray studies.
Authors I.Andersson, C.I.Brändén.
Ref. J Mol Biol, 1984, 172, 363-366.
PubMed id 6582279
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