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PDBsum entry 1bwv

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Lyase PDB id
1bwv
Jmol
Contents
Protein chains
472 a.a. *
138 a.a. *
Ligands
CAP ×4
Metals
_MG ×4
Waters ×542
* Residue conservation analysis

References listed in PDB file
Key reference
Title Crystal structure of carboxylase reaction-Oriented ribulose 1, 5-Bisphosphate carboxylase/oxygenase from a thermophilic red alga, Galdieria partita.
Authors H.Sugawara, H.Yamamoto, N.Shibata, T.Inoue, S.Okada, C.Miyake, A.Yokota, Y.Kai.
Ref. J Biol Chem, 1999, 274, 15655-15661.
PubMed id 10336462
Abstract
Ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco, EC 4.1.1. 39) obtained from a thermophilic red alga Galdieria partita has the highest specificity factor of 238 among the Rubiscos hitherto reported. Crystal structure of activated Rubisco from G. partita complexed with the reaction intermediate analogue, 2-carboxyarabinitol 1,5-bisphosphate (2-CABP) has been determined at 2.4-A resolution. Compared with other Rubiscos, different amino residues bring the structural differences in active site, which are marked around the binding sites of P-2 phosphate of 2-CABP. Especially, side chains of His-327 and Arg-295 show the significant differences from those of spinach Rubisco. Moreover, the side chains of Asn-123 and His-294 which are reported to bind the substrate, ribulose 1,5-bisphosphate, form hydrogen bonds characteristic of Galdieria Rubisco. Small subunits of Galdieria Rubisco have more than 30 extra amino acid residues on the C terminus, which make up a hairpin-loop structure to form many interactions with the neighboring small subunits. When the structures of Galdieria and spinach Rubiscos are superimposed, the hairpin region of the neighboring small subunit in Galdieria enzyme and apical portion of insertion residues 52-63 characteristic of small subunits in higher plant enzymes are almost overlapped to each other.
Secondary reference #1
Title Large structures at high resolution: the 1.6 a crystal structure of spinach ribulose-1,5-Bisphosphate carboxylase/oxygenase complexed with 2-Carboxyarabinitol bisphosphate.
Author I.Andersson.
Ref. J Mol Biol, 1996, 259, 160-174. [DOI no: 10.1006/jmbi.1996.0310]
PubMed id 8648644
Full text Abstract
Figure 1.
Figure 1. Reactions catalysed by rubisco.
Figure 7.
Figure 7. Overview of the active site of spinach rubisco showing 2-CABP, Mg 2+ and residues within hydrogen-bonding distance to these ligands. The hydroxyl groups at C2 and C3 of 2-CABP are in cis conformation. The two views in (a) and (b) are related by 180° with respect to the vertical axis.
The above figures are reproduced from the cited reference with permission from Elsevier
PROCHECK
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