2a5h: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:2a5h.gif|left|200px]] | [[Image:2a5h.gif|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_2a5h", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
or leave the SCENE parameter empty for the default display. | |||
--> | |||
{{STRUCTURE_2a5h| PDB=2a5h | SCENE= }} | |||
}} | |||
'''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).''' | ||
| Line 31: | Line 28: | ||
[[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 18:37, 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).
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. 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 Page seeded by OCA on Sat May 3 18:37:55 2008