2a5h
From Proteopedia
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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).''' | '''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).''' | ||
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[[Category: Ruzicka, F J.]] | [[Category: Ruzicka, F J.]] | ||
[[Category: 4fe4]] | [[Category: 4fe4]] | ||
- | [[Category: | + | [[Category: Alpha-beta channel]] |
- | [[Category: | + | [[Category: External aldimine]] |
- | [[Category: | + | [[Category: Four-iron-four-sulfur cluster]] |
- | [[Category: | + | [[Category: Fs4]] |
- | [[Category: | + | [[Category: Michaelis analog]] |
- | [[Category: | + | [[Category: Pyridoxal-5'-phosphate]] |
- | [[Category: | + | [[Category: Radical sam]] |
- | [[Category: | + | [[Category: S-adenosylmethionine]] |
- | [[Category: | + | [[Category: Sam]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:37:55 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 15:37, 3 May 2008
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).
Overview
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 Structure
2A5H is a Single protein structure of sequence from Clostridium subterminale. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Sat May 3 18:37:55 2008
Categories: Clostridium subterminale | Lysine 2,3-aminomutase | Single protein | Frey, P A. | Lepore, B W. | Ringe, D. | Ruzicka, F J. | 4fe4 | Alpha-beta channel | External aldimine | Four-iron-four-sulfur cluster | Fs4 | Michaelis analog | Pyridoxal-5'-phosphate | Radical sam | S-adenosylmethionine | Sam