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New page: left|200px<br /><applet load="1m6s" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m6s, resolution 1.8Å" /> '''Crystal Structure Of ...
 
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[[Image:1m6s.jpg|left|200px]]<br /><applet load="1m6s" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1m6s, resolution 1.8&Aring;" />
'''Crystal Structure Of Threonine Aldolase'''<br />


==Overview==
==Crystal Structure Of Threonine Aldolase==
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.
<StructureSection load='1m6s' size='340' side='right'caption='[[1m6s]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>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 [https://proteopedia.org/fgij/fg.htm?mol=1M6S FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1m6s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m6s OCA], [https://pdbe.org/1m6s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m6s RCSB], [https://www.ebi.ac.uk/pdbsum/1m6s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m6s ProSAT]</span></td></tr>
</table>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m6/1m6s_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1m6s ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


==About this Structure==
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>
1M6S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with CA and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Threonine_aldolase Threonine aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.5 4.1.2.5] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M6S OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12269813 12269813]
</div>
[[Category: Single protein]]
<div class="pdbe-citations 1m6s" style="background-color:#fffaf0;"></div>
[[Category: Thermotoga maritima]]
[[Category: Threonine aldolase]]
[[Category: Burley, S.K.]]
[[Category: Kielkopf, C.L.]]
[[Category: CA]]
[[Category: CL]]
[[Category: enzyme]]
[[Category: plp]]
[[Category: pyridoxal phosphate]]
[[Category: threonine]]
[[Category: vitamin b12]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 03:53:09 2007''
==See Also==
*[[Aldolase 3D structures|Aldolase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Burley SK]]
[[Category: Kielkopf CL]]
Retrieved from "https://proteopedia.org/1m6s"