9cq5

Mn-bound RuBisCO from spinach with CABP inhibitor

spinqualitylabelsall models 9cq5, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9cq5 is a 16 chain structure with sequence from Spinacia oleracea. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.5Å Ligands: CAP, KCX, MN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RBL_SPIOL RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.[HAMAP-Rule:MF_01338] Publication Abstract from PubMed The rate of photosynthesis and, thus, CO(2) fixation, is limited by the rate of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco). Not only does Rubisco have a relatively low catalytic rate, but it also is promiscuous regarding the metal identity in the active site of the large subunit. In Nature, Rubisco binds either Mg(II) or Mn(II), depending on the chloroplastic ratio of these metal ions; most studies performed with Rubisco have focused on Mg-bound Rubisco. Herein, we report the first crystal structure of a Mn-bound Rubisco, and we compare its structural properties to those of its Mg-bound analogues. The structure of Mn(II)-bound Rubisco from Spinacia oleracea.,Voland RW, Coleman RE, Lancaster KM J Inorg Biochem. 2024 Nov;260:112682. doi: 10.1016/j.jinorgbio.2024.112682. Epub , 2024 Jul 30. PMID:39094246 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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