1m6s

<StructureSection load='1m6s' size='340' side='right'caption='[[1m6s]], [[Resolution|resolution]] 1.80&Aring;' scene=''>

<table><tr><td colspan='2'>[[1m6s]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M6S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1M6S FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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=1m6s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m6s OCA], [http://pdbe.org/1m6s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1m6s RCSB], [http://www.ebi.ac.uk/pdbsum/1m6s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1m6s ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

L-Threonine acetaldehyde-lyase (threonine aldolase, TA) is a pyridoxal-5'-phosphate-dependent (PLP) enzyme that catalyzes conversion of L-threonine or L-allo-threonine to glycine and acetaldehyde in a secondary glycine biosynthetic pathway. X-ray structures of Thermatoga maritima TA have been determined as the apo-enzyme at 1.8 A resolution and bound to substrate L-allo-threonine and product glycine at 1.9 and 2.0 A resolution, respectively. Despite low pairwise sequence identities, TA is a member of aspartate aminotransferase (AATase) fold family of PLP enzymes. The enzyme forms a 222 homotetramer with the PLP cofactor bound via a Schiff-base linkage to Lys199 within a domain interface. The structure reveals bound calcium and chloride ions that appear to contribute to catalysis and oligomerization, respectively. Although L-threonine and L-allo-threonine are substrates for T. maritima TA, enzymatic assays revealed a strong preference for L-allo-threonine. Structures of the external aldimines with substrate/product reveal a pair of histidines that may provide flexibility in substrate recognition. Variation in the threonine binding pocket may explain preferences for L-allo-threonine versus L-threonine among TA family members.

X-ray structures of threonine aldolase complexes: structural basis of substrate recognition.,Kielkopf CL, Burley SK Biochemistry. 2002 Oct 1;41(39):11711-20. PMID:12269813<ref>PMID:12269813</ref>

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

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<div class="pdbe-citations 1m6s" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Atcc 43589]]

[[Category: L-threonine aldolase]]

[[Category: Burley, S K]]

[[Category: Kielkopf, C L]]

[[Category: Vitamin b12]]