9CQ5

Mn-bound RuBisCO from spinach with CABP inhibitor

Summary for 9CQ5

Entry DOI	10.2210/pdb9cq5/pdb
Descriptor	Ribulose bisphosphate carboxylase large chain, Ribulose bisphosphate carboxylase small subunit, chloroplastic 2, MANGANESE (II) ION, ... (5 entities in total)
Functional Keywords	carboxylase, oxygenase, inhibitor, manganese, photosynthesis, plant protein
Biological source	Spinacia oleracea (spinach) More
Total number of polymer chains	16
Total formula weight	543195.73
Authors	Voland, R.W.,Lancaster, K.M. (deposition date: 2024-07-19, release date: 2025-02-05)
Primary citation	Voland, R.W.,Coleman, R.E.,Lancaster, K.M. The structure of Mn(II)-bound Rubisco from Spinacia oleracea. J.Inorg.Biochem., 260:112682-112682, 2024 Cited by PubMed Abstract: The rate of photosynthesis and, thus, CO 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. PubMed: 39094246 DOI: 10.1016/j.jinorgbio.2024.112682 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.5 Å)

Structure validation