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1ag1

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(New page: 200px<br /><applet load="1ag1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ag1, resolution 2.36&Aring;" /> '''MONOHYDROGEN PHOSPHA...)
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[[Image:1ag1.jpg|left|200px]]<br /><applet load="1ag1" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ag1, resolution 2.36&Aring;" />
 
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'''MONOHYDROGEN PHOSPHATE BINDING TO TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE'''<br />
 
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==Overview==
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==MONOHYDROGEN PHOSPHATE BINDING TO TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE==
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The three-dimensional structure of triosephosphate isomerase complexed, with the competitive inhibitor SO-4(2) was determined by X-ray, crystallography to a resolution of 0.24 nm. A comparison with the native, crystal structure, where SO-4(2) is bound, revealed five changes: (a) a, 0.10-nm shift of the anion-binding site; (b) a further closing of the, flexible loop of the enzyme; (c) a 'swinging in' of the side chain of the, catalytic Glu, that is chi 1 changes from (+) to (-) synclinal; (d) an, altered water structure; (e) a disappearance of the conformational, heterogeneity at the C-terminus of strand beta 7. Some of these changes, may be related to the different hydrogen-bond pattern about the two, different anions. However, the distance of 0.10 nm between the sulphur and, phosphorus positions is unexpected and remains intriguing.
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<StructureSection load='1ag1' size='340' side='right'caption='[[1ag1]], [[Resolution|resolution]] 2.36&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ag1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Trypanosoma_brucei Trypanosoma brucei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AG1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AG1 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]] 2.36&#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=PO4:PHOSPHATE+ION'>PO4</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=1ag1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ag1 OCA], [https://pdbe.org/1ag1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ag1 RCSB], [https://www.ebi.ac.uk/pdbsum/1ag1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ag1 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TPIS_TRYBB TPIS_TRYBB]
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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/ag/1ag1_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=1ag1 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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The three-dimensional structure of triosephosphate isomerase complexed with the competitive inhibitor SO-4(2) was determined by X-ray crystallography to a resolution of 0.24 nm. A comparison with the native crystal structure, where SO-4(2) is bound, revealed five changes: (a) a 0.10-nm shift of the anion-binding site; (b) a further closing of the flexible loop of the enzyme; (c) a 'swinging in' of the side chain of the catalytic Glu, that is chi 1 changes from (+) to (-) synclinal; (d) an altered water structure; (e) a disappearance of the conformational heterogeneity at the C-terminus of strand beta 7. Some of these changes may be related to the different hydrogen-bond pattern about the two different anions. However, the distance of 0.10 nm between the sulphur and phosphorus positions is unexpected and remains intriguing.
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==About this Structure==
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Anion binding at the active site of trypanosomal triosephosphate isomerase. Monohydrogen phosphate does not mimic sulphate.,Verlinde CL, Noble ME, Kalk KH, Groendijk H, Wierenga RK, Hol WG Eur J Biochem. 1991 May 23;198(1):53-7. PMID:2040290<ref>PMID:2040290</ref>
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1AG1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Trypanosoma_brucei Trypanosoma brucei] with PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Triose-phosphate_isomerase Triose-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.1 5.3.1.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AG1 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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Anion binding at the active site of trypanosomal triosephosphate isomerase. Monohydrogen phosphate does not mimic sulphate., Verlinde CL, Noble ME, Kalk KH, Groendijk H, Wierenga RK, Hol WG, Eur J Biochem. 1991 May 23;198(1):53-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2040290 2040290]
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</div>
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[[Category: Single protein]]
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<div class="pdbe-citations 1ag1" style="background-color:#fffaf0;"></div>
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[[Category: Triose-phosphate isomerase]]
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[[Category: Trypanosoma brucei]]
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[[Category: Hol, W.G.J.]]
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[[Category: Verlinde, C.L.M.J.]]
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[[Category: PO4]]
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[[Category: isomerase (intramolecular oxidoreductase)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:49:31 2007''
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==See Also==
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*[[Triose phosphate isomerase 3D structures|Triose phosphate isomerase 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: Trypanosoma brucei]]
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[[Category: Hol WGJ]]
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[[Category: Verlinde CLMJ]]

Current revision

MONOHYDROGEN PHOSPHATE BINDING TO TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE

PDB ID 1ag1

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