2a5h: Difference between revisions

New page: left|200px<br /><applet load="2a5h" size="450" color="white" frame="true" align="right" spinBox="true" caption="2a5h, resolution 2.10Å" /> '''2.1 Angstrom X-ray c...
 
No edit summary
Line 1: Line 1:
[[Image:2a5h.gif|left|200px]]<br /><applet load="2a5h" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2a5h.gif|left|200px]]<br /><applet load="2a5h" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2a5h, resolution 2.10&Aring;" />
caption="2a5h, resolution 2.10&Aring;" />
'''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).'''<br />
'''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).'''<br />


==Overview==
==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.
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==
==About this Structure==
2A5H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_subterminale Clostridium subterminale] with ZN, SO4, SAM, LYS and SF4 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Lysine_2,3-aminomutase Lysine 2,3-aminomutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.3.2 5.4.3.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2A5H OCA].  
2A5H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_subterminale Clostridium subterminale] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=SAM:'>SAM</scene>, <scene name='pdbligand=LYS:'>LYS</scene> and <scene name='pdbligand=SF4:'>SF4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Lysine_2,3-aminomutase Lysine 2,3-aminomutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.3.2 5.4.3.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A5H OCA].  


==Reference==
==Reference==
Line 14: Line 14:
[[Category: Lysine 2,3-aminomutase]]
[[Category: Lysine 2,3-aminomutase]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Frey, P.A.]]
[[Category: Frey, P A.]]
[[Category: Lepore, B.W.]]
[[Category: Lepore, B W.]]
[[Category: Ringe, D.]]
[[Category: Ringe, D.]]
[[Category: Ruzicka, F.J.]]
[[Category: Ruzicka, F J.]]
[[Category: LYS]]
[[Category: LYS]]
[[Category: SAM]]
[[Category: SAM]]
Line 34: Line 34:
[[Category: sam]]
[[Category: sam]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:55:42 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:23:47 2008''

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA