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PDBsum entry 1rbl

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Lyase PDB id
1rbl
Jmol
Contents
Protein chains
(+ 2 more) 467 a.a. *
(+ 2 more) 109 a.a. *
Ligands
CAP ×8
FMT ×8
Metals
_MG ×8
Waters ×292
* Residue conservation analysis

References listed in PDB file
Key reference
Title Structure determination and refinement of ribulose 1,5-Bisphosphate carboxylase/oxygenase from synechococcus pcc6301.
Authors J.Newman, C.I.Branden, T.A.Jones.
Ref. Acta Crystallogr D Biol Crystallogr, 1993, 49, 548-560. [DOI no: 10.1107/S090744499300530X]
PubMed id 15299492
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 81%.
Abstract
The structure of an activated quaternary complex of ribulose 1,5-bisphosphate carboxylase/oxygenase (rubisco) from Synechococcus PCC6301 has been solved by molecular replacement. The protein crystallizes in an orthorhombic P2(1)2(1)2(1) unit cell with a complete L(8)S(8) complex consisting of 4608 residues (37 680 non-hydrogen atoms) in the asymmetric unit. Data were collected both on film and image plate using synchrotron radiation; there were 218 276 unique reflections in the final 2.2 A data set. The eightfold non-crystallographic symmetry could be used both to improve map quality and to reduce the computing requirements of refinement. The coordinates were refined using strict non-crystallographic symmetry constraints. The stereochemistry of the final model is good, and the model has an R value of 20.0% for the reflections between 7 and 2.2 A.
Figure 9.
Fig. 9. A ribbon diagram of an/,2 dimer. The barrel of one L subunit is coloured blue, and the N-terminal domain of the same subunit, cyan. The barrel domain of the second L subunit is red, and its N-terminal domain is magenta. The yellow spheres are Mg 2 ions, and show the positions of the active sites. Both this figure and the previous figure were generated in O.
Figure 15.
Fig. 15. Pepflip values versus residue number. The dashed line shows the 2.5 threshold suggested by Jones et al. Table 3 summarizes the residues which have~ a pepflip >__ 2.5.
The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (1993, 49, 548-560) copyright 1993.
Secondary reference #1
Title The X-Ray structure of synechococcus ribulose-Bisphosphate carboxylase/oxygenase-Activated quaternary complex at 2.2-A resolution.
Authors J.Newman, S.Gutteridge.
Ref. J Biol Chem, 1993, 268, 25876-25886.
PubMed id 8245022
Note: In the PDB file this reference is annotated as "TO BE PUBLISHED". The citation details given above were obtained from the PDBe's Unpublished References server.
Abstract
PROCHECK
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