4au1 | pdb_00004au1

Crystal Structure of CobH (precorrin-8x methyl mutase) complexed with C5 desmethyl-HBA

spinqualitylabelsall models 4au1, resolution 1.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4au1 is a 1 chain structure with sequence from Rhodobacter capsulatus SB 1003. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.45Å Ligands: P8X, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function D5AV08_RHOCB Publication Abstract from PubMed 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. An enzyme-trap approach allows isolation of intermediates in cobalamin biosynthesis.,Deery E, Schroeder S, Lawrence AD, Taylor SL, Seyedarabi A, Waterman J, Wilson KS, Brown D, Geeves MA, Howard MJ, Pickersgill RW, Warren MJ Nat Chem Biol. 2012 Oct 7. doi: 10.1038/nchembio.1086. PMID:23042036 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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