1cj0

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(New page: 200px<br /><applet load="1cj0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cj0, resolution 2.80&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1cj0.gif|left|200px]]<br /><applet load="1cj0" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1cj0, resolution 2.80&Aring;" />
 
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'''CRYSTAL STRUCTURE OF RABBIT CYTOSOLIC SERINE HYDROXYMETHYLTRANSFERASE AT 2.8 ANGSTROM RESOLUTION'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF RABBIT CYTOSOLIC SERINE HYDROXYMETHYLTRANSFERASE AT 2.8 ANGSTROM RESOLUTION==
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Serine hydroxymethyltransferase (SHMT) catalyzes the reversible cleavage, of serine to form glycine and single carbon groups that are essential for, many biosynthetic pathways. SHMT requires both pyridoxal phosphate (PLP), and tetrahydropteroylpolyglutamate (H4PteGlun) as cofactors, the latter as, a carrier of the single carbon group. We describe here the crystal, structure at 2.8 A resolution of rabbit cytosolic SHMT (rcSHMT) in two, forms: one with the PLP covalently bound as an aldimine to the, Nepsilon-amino group of the active site lysine and the other with the, aldimine reduced to a secondary amine. The rcSHMT structure closely, resembles the structure of human SHMT, confirming its similarity to the, alpha-class of PLP enzymes. The structures reported here further permit, identification of changes in the PLP group that accompany formation of the, geminal diamine complex, the first intermediate in the reaction pathway., On the basis of the current mechanism derived from solution studies and, the properties of site mutants, we are able to model the binding of both, the serine substrate and the H4PteGlun cofactor. This model explains the, properties of several site mutants of SHMT and offers testable hypotheses, for a more detailed mechanism of this enzyme.
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<StructureSection load='1cj0' size='340' side='right'caption='[[1cj0]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1cj0]] is a 2 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=1CJ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CJ0 FirstGlance]. <br>
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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]] 2.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
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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=1cj0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cj0 OCA], [https://pdbe.org/1cj0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cj0 RCSB], [https://www.ebi.ac.uk/pdbsum/1cj0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cj0 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GLYC_RABIT GLYC_RABIT] Interconversion of serine and glycine.
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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/cj/1cj0_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=1cj0 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Serine hydroxymethyltransferase (SHMT) catalyzes the reversible cleavage of serine to form glycine and single carbon groups that are essential for many biosynthetic pathways. SHMT requires both pyridoxal phosphate (PLP) and tetrahydropteroylpolyglutamate (H4PteGlun) as cofactors, the latter as a carrier of the single carbon group. We describe here the crystal structure at 2.8 A resolution of rabbit cytosolic SHMT (rcSHMT) in two forms: one with the PLP covalently bound as an aldimine to the Nepsilon-amino group of the active site lysine and the other with the aldimine reduced to a secondary amine. The rcSHMT structure closely resembles the structure of human SHMT, confirming its similarity to the alpha-class of PLP enzymes. The structures reported here further permit identification of changes in the PLP group that accompany formation of the geminal diamine complex, the first intermediate in the reaction pathway. On the basis of the current mechanism derived from solution studies and the properties of site mutants, we are able to model the binding of both the serine substrate and the H4PteGlun cofactor. This model explains the properties of several site mutants of SHMT and offers testable hypotheses for a more detailed mechanism of this enzyme.
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==About this Structure==
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Crystal structure of rabbit cytosolic serine hydroxymethyltransferase at 2.8 A resolution: mechanistic implications.,Scarsdale JN, Kazanina G, Radaev S, Schirch V, Wright HT Biochemistry. 1999 Jun 29;38(26):8347-58. PMID:10387080<ref>PMID:10387080</ref>
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1CJ0 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 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CJ0 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Crystal structure of rabbit cytosolic serine hydroxymethyltransferase at 2.8 A resolution: mechanistic implications., Scarsdale JN, Kazanina G, Radaev S, Schirch V, Wright HT, Biochemistry. 1999 Jun 29;38(26):8347-58. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10387080 10387080]
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</div>
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[[Category: Oryctolagus cuniculus]]
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<div class="pdbe-citations 1cj0" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Kazanina, G.]]
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[[Category: Radaev, S.]]
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[[Category: Scarsdale, J.N.]]
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[[Category: Schirch, V.]]
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[[Category: Wright, H.T.]]
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[[Category: PLP]]
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[[Category: 1 carbon metabolism]]
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[[Category: hydroxymethyl transferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:30:17 2007''
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==See Also==
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*[[Serine hydroxymethyltransferase 3D structures|Serine hydroxymethyltransferase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Oryctolagus cuniculus]]
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[[Category: Kazanina G]]
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[[Category: Radaev S]]
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[[Category: Scarsdale JN]]
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[[Category: Schirch V]]
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[[Category: Wright HT]]

Current revision

CRYSTAL STRUCTURE OF RABBIT CYTOSOLIC SERINE HYDROXYMETHYLTRANSFERASE AT 2.8 ANGSTROM RESOLUTION

PDB ID 1cj0

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