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New page: left|200px<br /><applet load="1ls3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ls3, resolution 2.70Å" /> '''Crystal Structure of...
 
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[[Image:1ls3.gif|left|200px]]<br /><applet load="1ls3" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1ls3, resolution 2.70&Aring;" />
'''Crystal Structure of the Complex between Rabbit Cytosolic Serine Hydroxymethyltransferase and TriGlu-5-formyl-tetrahydrofolate'''<br />


==Overview==
==Crystal Structure of the Complex between Rabbit Cytosolic Serine Hydroxymethyltransferase and TriGlu-5-formyl-tetrahydrofolate==
Serine hydroxymethyltransferase (SHMT; EC 2.1.2.1) catalyzes the, reversible interconversion of serine and glycine with transfer of the, serine side chain one-carbon group to tetrahydropteroylglutamate, (H(4)PteGlu), and also the conversion of 5,10-methenyl-H(4)PteGlu to, 5-formyl-H(4)PteGlu. In the cell, H(4)PteGlu carries a poly-gamma-glutamyl, tail of at least 3 glutamyl residues that is required for physiological, activity. This study combines solution binding and mutagenesis studies, with crystallographic structure determination to identify the extended, binding site for tetrahydropteroylpolyglutamate on rabbit cytosolic SHMT., Equilibrium binding and kinetic measurements of H(4)PteGlu(3) and, H(4)PteGlu(5) with wild-type and Lys --&gt; Gln or Glu site mutant, homotetrameric rabbit cytosolic SHMTs identified lysine residues that, contribute to the binding of the polyglutamate tail. The crystal structure, of the enzyme in complex with 5-formyl-H(4)PteGlu(3) confirms the solution, data and indicates that the conformation of the pteridine ring and its, interactions with the enzyme differ slightly from those observed in, complexes of the monoglutamate cofactor. The polyglutamate chain, which, does not contribute to catalysis, exists in multiple conformations in each, of the two occupied binding sites and appears to be bound by the, electrostatic field created by the cationic residues, with only limited, interactions with specific individual residues.
<StructureSection load='1ls3' size='340' side='right'caption='[[1ls3]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ls3]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LS3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LS3 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]] 2.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=TGF:2-[4-(4-{4-[(2-AMINO-5-FORMYL-4-OXO-3,4,5,6,7,8-HEXAHYDRO-PTERIDIN-6-YLMETHYL)-AMINO]-BENZOYLAMINO}-4-CARBOXY-BUTYRYLAMINO)-4-CARBOXY-BUTYRYLAMINO]-PENTANEDIOIC+ACID'>TGF</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=1ls3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ls3 OCA], [https://pdbe.org/1ls3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ls3 RCSB], [https://www.ebi.ac.uk/pdbsum/1ls3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ls3 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GLYC_RABIT GLYC_RABIT] Interconversion of serine and glycine.
== 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/ls/1ls3_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1ls3 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1LS3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with PLP, PLP, TGF and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Glycine_hydroxymethyltransferase Glycine hydroxymethyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.1 2.1.2.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LS3 OCA].
*[[Serine hydroxymethyltransferase 3D structures|Serine hydroxymethyltransferase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Location of the pteroylpolyglutamate-binding site on rabbit cytosolic serine hydroxymethyltransferase., Fu TF, Scarsdale JN, Kazanina G, Schirch V, Wright HT, J Biol Chem. 2003 Jan 24;278(4):2645-53. Epub 2002 Nov 15. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12438316 12438316]
[[Category: Large Structures]]
[[Category: Glycine hydroxymethyltransferase]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
[[Category: Single protein]]
[[Category: Fu TF]]
[[Category: Fu, T.F.]]
[[Category: Kazanina G]]
[[Category: Kazanina, G.]]
[[Category: Scarsdale JN]]
[[Category: Scarsdale, J.N.]]
[[Category: Schirch V]]
[[Category: Schirch, V.]]
[[Category: Wright HT]]
[[Category: Wright, H.T.]]
[[Category: GOL]]
[[Category: PLP]]
[[Category: TGF]]
[[Category: asymmetric tetramer]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:49:42 2007''

Latest revision as of 06:06, 3 April 2024

Crystal Structure of the Complex between Rabbit Cytosolic Serine Hydroxymethyltransferase and TriGlu-5-formyl-tetrahydrofolate

1ls3, resolution 2.70Å

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