2a5h
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2.1 Angstrom X-ray crystal structure of lysine-2,3-aminomutase from Clostridium subterminale SB4, with Michaelis analog (L-alpha-lysine external aldimine form of pyridoxal-5'-phosphate).
OverviewOverview
The x-ray crystal structure of the pyridoxal-5'-phosphate (PLP), S-adenosyl-L-methionine (SAM), and [4Fe-4S]-dependent, lysine-2,3-aminomutase (LAM) of Clostridium subterminale has been solved, to 2.1-A resolution by single-wavelength anomalous dispersion methods on a, L-selenomethionine-substituted complex of LAM with [4Fe-4S]2+, PLP, SAM, and L-alpha-lysine, a very close analog of the active Michaelis complex., The unit cell contains a dimer of hydrogen-bonded, domain-swapped dimers, the subunits of which adopt a fold that contains all three cofactors in a, central channel defined by six beta/alpha structural units. Zinc, coordination links the domain-swapped dimers. In each subunit, the solvent, face of the channel is occluded by an N-terminal helical domain, with the, opposite end of the channel packed against the domain-swapped subunit., Hydrogen-bonded ionic contacts hold the external aldimine of PLP and, L-alpha-lysine in position for abstraction of the 3-pro-R hydrogen of, lysine by C5' of SAM. The structure of the SAM/[4Fe-4S] complex confirms, and extends conclusions from spectroscopic studies of LAM and shows, selenium in Se-adenosyl-L-selenomethionine poised to ligate the unique, iron in the [4Fe-4S] cluster upon electron transfer and radical formation., The chain fold in the central domain is in part analogous to other, radical-SAM enzymes.
About this StructureAbout this Structure
2A5H is a Single protein structure of sequence from Clostridium subterminale with ZN, SO4, SAM, LYS and SF4 as ligands. Active as Lysine 2,3-aminomutase, with EC number 5.4.3.2 Full crystallographic information is available from OCA.
ReferenceReference
The x-ray crystal structure of lysine-2,3-aminomutase from Clostridium subterminale., Lepore BW, Ruzicka FJ, Frey PA, Ringe D, Proc Natl Acad Sci U S A. 2005 Sep 27;102(39):13819-24. Epub 2005 Sep 15. PMID:16166264
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