PDBsum entry 1gk8

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Lyase PDB id
Protein chains
469 a.a. *
126 a.a. *
CAP ×4
EDO ×33
_MG ×4
Waters ×2556
* Residue conservation analysis

References listed in PDB file
Key reference
Title First crystal structure of rubisco from a green alga, Chlamydomonas reinhardtii.
Authors T.C.Taylor, A.Backlund, K.Bjorhall, R.J.Spreitzer, I.Andersson.
Ref. J Biol Chem, 2001, 276, 48159-48164. [DOI no: 10.1074/jbc.M107765200]
PubMed id 11641402
The crystal structure of Rubisco (ribulose 1,5-bisphosphate carboxylase/oxygenase) from the unicellular green alga Chlamydomonas reinhardtii has been determined to 1.4 A resolution. Overall, the structure shows high similarity to the previously determined structures of L8S8 Rubisco enzymes. The largest difference is found in the loop between beta strands A and B of the small subunit (betaA-betaB loop), which is longer by six amino acid residues than the corresponding region in Rubisco from Spinacia. Mutations of residues in the betaA-betaB loop have been shown to affect holoenzyme stability and catalytic properties. The information contained in the Chlamydomonas structure enables a more reliable analysis of the effect of these mutations. No electron density was observed for the last 13 residues of the small subunit, which are assumed to be disordered in the crystal. Because of the high resolution of the data, some posttranslational modifications are unambiguously apparent in the structure. These include cysteine and N-terminal methylations and proline 4-hydroxylations.
Figure 4.
Fig. 4. Electron density ( 2mF[o] DF[c] contoured at 1 ) for the A- B loop of the S subunit. Alternate conformations for the O of Ser-64 and S of Cys-65 are shown in dark red and green, respectively.
Figure 5.
Fig. 5. Representative electron density for modified residues. A, S-methylcysteine; B, 4-hydroxyproline; and C, N-methylmethionine.
The above figures are reprinted by permission from the ASBMB: J Biol Chem (2001, 276, 48159-48164) copyright 2001.
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