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1m6s

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[[Image:1m6s.jpg|left|200px]]
 
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{{Structure
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==Crystal Structure Of Threonine Aldolase==
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|PDB= 1m6s |SIZE=350|CAPTION= <scene name='initialview01'>1m6s</scene>, resolution 1.8&Aring;
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<StructureSection load='1m6s' size='340' side='right'caption='[[1m6s]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene>
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<table><tr><td colspan='2'>[[1m6s]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. 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>
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|ACTIVITY= [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]
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</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>
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|GENE=
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<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>
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}}
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<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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q9X266_THEMA Q9X266_THEMA]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m6/1m6s_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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'''Crystal Structure Of Threonine Aldolase'''
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==See Also==
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*[[Aldolase 3D structures|Aldolase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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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.
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[[Category: Large Structures]]
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==About this Structure==
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1M6S is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M6S OCA].
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==Reference==
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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://www.ncbi.nlm.nih.gov/pubmed/12269813 12269813]
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[[Category: Single protein]]
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[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
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[[Category: Threonine aldolase]]
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[[Category: Burley SK]]
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[[Category: Burley, S K.]]
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[[Category: Kielkopf CL]]
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[[Category: Kielkopf, C L.]]
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[[Category: CA]]
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[[Category: CL]]
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[[Category: enzyme]]
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[[Category: plp]]
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[[Category: pyridoxal phosphate]]
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[[Category: threonine]]
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[[Category: vitamin b12]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:39:41 2008''
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Current revision

Crystal Structure Of Threonine Aldolase

PDB ID 1m6s

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