3kp0

<table><tr><td colspan='2'>[[3kp0]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Acest Acest]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KP0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KP0 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5AD:5-DEOXYADENOSINE'>5AD</scene>, <scene name='pdbligand=B12:COBALAMIN'>B12</scene>, <scene name='pdbligand=Z98:(2S)-2-AMINO-4-{[(1Z)-{3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYLIDENE]AMINO}BUTANOIC+ACID'>Z98</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">oraE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1511 ACEST]), oraS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1511 ACEST])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3kp0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kp0 OCA], [http://pdbe.org/3kp0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3kp0 RCSB], [http://www.ebi.ac.uk/pdbsum/3kp0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3kp0 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/OAME_CLOSD OAME_CLOSD]] Component of a complex that catalyzes the reversible migration of the omega amino group of D-ornithine to C-4 to form (2R,4S)-2,4-diaminopentanoic acid. OraE may be the catalytic subunit. Active only on D-ornithine and 2,4-diaminopentanoic acid but not active on L-ornithine, L-beta-lysine, L-alpha-lysine or D-alpha-lysine.<ref>PMID:11577113</ref> <ref>PMID:4711468</ref> <ref>PMID:11577113</ref> [[http://www.uniprot.org/uniprot/OAMS_CLOSD OAMS_CLOSD]] Component of a complex that catalyzes the reversible migration of the omega amino group of D-ornithine to C-4 to form (2R,4S)-2,4-diaminopentanoic acid. The role of OraS remains obscure; however, it seems to be required for a correct folding of the OraE subunit. The complex is active only on D-ornithine and 2,4-diaminopentanoic acid and not active on L-ornithine, L-beta-lysine, L-alpha-lysine or D-alpha-lysine.<ref>PMID:11577113</ref> <ref>PMID:4711468</ref> <ref>PMID:4711468</ref>

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

D-ornithine 4,5-aminomutase (OAM) from Clostridium sticklandii converts D-ornithine to 2,4-diaminopentanoic acid by way of radical propagation from an adenosylcobalamin (AdoCbl) to a pyridoxal 5'-phosphate (PLP) cofactor. We have solved OAM crystal structures in different catalytic states that together demonstrate unusual stability of the AdoCbl Co-C bond and that radical catalysis is coupled to large-scale domain motion. The 2.0-A substrate-free enzyme crystal structure reveals the Rossmann domain, harboring the intact AdoCbl cofactor, is tilted toward the edge of the PLP binding triose-phosphate isomerase barrel domain. The PLP forms an internal aldimine link to the Rossmann domain through Lys(629), effectively locking the enzyme in this "open" pre-catalytic conformation. The distance between PLP and 5'-deoxyadenosyl group is 23 A, and large-scale domain movement is thus required prior to radical catalysis. The OAM crystals contain two Rossmann domains within the asymmetric unit that are unconstrained by the crystal lattice. Surprisingly, the binding of various ligands to OAM crystals (in an oxygen-free environment) leads to transimination in the absence of significant reorientation of the Rossmann domains. In contrast, when performed under aerobic conditions, this leads to extreme disorder in the latter domains correlated with the loss of the 5'-deoxyadenosyl group. Our data indicate turnover and hence formation of the "closed" conformation is occurring within OAM crystals, but that the equilibrium is poised toward the open conformation. We propose that substrate binding induces large-scale domain motion concomitant with a reconfiguration of the 5'-deoxyadenosyl group, triggering radical catalysis in OAM.

Large-scale domain dynamics and adenosylcobalamin reorientation orchestrate radical catalysis in ornithine 4,5-aminomutase.,Wolthers KR, Levy C, Scrutton NS, Leys D J Biol Chem. 2010 Apr 30;285(18):13942-50. Epub 2010 Jan 27. PMID:20106986<ref>PMID:20106986</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 3kp0" style="background-color:#fffaf0;"></div>

[[Category: Acest]]

[[Category: Levy, C W]]

[[Category: Leys, D]]

[[Category: Scrutton, N S]]

[[Category: Wolthers, K R]]

[[Category: Metal binding protein]]