3NJR

Crystal structure of C-terminal domain of precorrin-6Y C5,15-methyltransferase from Rhodobacter capsulatus

Summary for 3NJR

• Entry DOI: 10.2210/pdb3njr/pdb
• Descriptor: Precorrin-6y methylase, S-ADENOSYL-L-HOMOCYSTEINE, GLYCEROL, ... (5 entities in total)
• Functional Keywords: methyltransferase, decarboxylase, transferase
• Biological source: Rhodobacter capsulatus
• Total number of polymer chains: 2
• Total formula weight: 45181.11

Authors

Seyedarabi, A.,Pickersgill, R.W. (deposition date: 2010-06-17, release date: 2011-06-08, Last modification date: 2023-09-06)

Primary citation

Deery, E.,Schroeder, S.,Lawrence, A.D.,Taylor, S.L.,Seyedarabi, A.,Waterman, J.,Wilson, K.S.,Brown, D.,Geeves, M.A.,Howard, M.J.,Pickersgill, R.W.,Warren, M.J.
An enzyme-trap approach allows isolation of intermediates in cobalamin biosynthesis.
Nat.Chem.Biol., 8:933-940, 2012

PubMed Abstract: The biosynthesis of many vitamins and coenzymes has often proven difficult to elucidate owing to a combination of low abundance and kinetic lability of the pathway intermediates. Through a serial reconstruction of the cobalamin (vitamin B(12)) pathway in Escherichia coli and by His tagging the terminal enzyme in the reaction sequence, we have observed that many unstable intermediates can be isolated as tightly bound enzyme-product complexes. Together, these approaches have been used to extract intermediates between precorrin-4 and hydrogenobyrinic acid in their free acid form and permitted the delineation of the overall reaction catalyzed by CobL, including the formal elucidation of precorrin-7 as a metabolite. Furthermore, a substrate-carrier protein, CobE, that can also be used to stabilize some of the transient metabolic intermediates and enhance their onward transformation, has been identified. The tight association of pathway intermediates with enzymes provides evidence for a form of metabolite channeling.

PubMed: 23042036
DOI: 10.1038/nchembio.1086

Experimental method

X-RAY DIFFRACTION (2.7 Å)