1if2

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Current revision (07:34, 7 February 2024) (edit) (undo)
 
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<StructureSection load='1if2' size='340' side='right'caption='[[1if2]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='1if2' size='340' side='right'caption='[[1if2]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1if2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Leime Leime]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IF2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IF2 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1if2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Leishmania_mexicana Leishmania mexicana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IF2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IF2 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=129:[2(FORMYL-HYDROXY-AMINO)-ETHYL]-PHOSPHONIC+ACID'>129</scene></td></tr>
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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&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Triose-phosphate_isomerase Triose-phosphate isomerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.1 5.3.1.1] </span></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=129:[2(FORMYL-HYDROXY-AMINO)-ETHYL]-PHOSPHONIC+ACID'>129</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=1if2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1if2 OCA], [https://pdbe.org/1if2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1if2 RCSB], [https://www.ebi.ac.uk/pdbsum/1if2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1if2 ProSAT]</span></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=1if2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1if2 OCA], [https://pdbe.org/1if2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1if2 RCSB], [https://www.ebi.ac.uk/pdbsum/1if2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1if2 ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TPIS_LEIME TPIS_LEIME]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1if2 ConSurf].
</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=1if2 ConSurf].
<div style="clear:both"></div>
<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 crystal structure of leishmania triosephosphate isomerase (TIM) complexed with 2-(N-formyl-N-hydroxy)-aminoethyl phosphonate (IPP) highlights the importance of Asn11 for binding and catalysis. IPP is an analogue of the substrate D-glyceraldehyde-3-phosphate, and it is observed to bind with its aldehyde oxygen in an oxyanion hole formed by ND2 of Asn11 and NE2 of His95. Comparison of the mode of binding of IPP and the transition state analogue phosphoglycolohydroxamate (PGH) suggests that the Glu167 side chain, as well as the triose part of the substrate, adopt different conformations as the catalysed reaction proceeds. Comparison of the TIM-IPP and the TIM-PGH structures with other liganded and unliganded structures also highlights the conformational flexibility of the ligand and the active site, as well as the conserved mode of ligand binding.
 
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Structural determinants for ligand binding and catalysis of triosephosphate isomerase.,Kursula I, Partanen S, Lambeir AM, Antonov DM, Augustyns K, Wierenga RK Eur J Biochem. 2001 Oct;268(19):5189-96. PMID:11589711<ref>PMID:11589711</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1if2" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Triose phosphate isomerase 3D structures|Triose phosphate isomerase 3D structures]]
*[[Triose phosphate isomerase 3D structures|Triose phosphate isomerase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Leime]]
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[[Category: Leishmania mexicana]]
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[[Category: Triose-phosphate isomerase]]
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[[Category: Antonov DM]]
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[[Category: Antonov, D M]]
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[[Category: Augustyns K]]
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[[Category: Augustyns, K]]
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[[Category: Kursula I]]
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[[Category: Kursula, I]]
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[[Category: Lambeir A-M]]
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[[Category: Lambeir, A M]]
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[[Category: Partanen S]]
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[[Category: Partanen, S]]
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[[Category: Wierenga RK]]
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[[Category: Wierenga, R K]]
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[[Category: Isomerase]]
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[[Category: Tim barrel]]
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[[Category: Transition state analogue]]
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Current revision

X-RAY STRUCTURE OF LEISHMANIA MEXICANA TRIOSEPHOSPHATE ISOMERASE COMPLEXED WITH IPP

PDB ID 1if2

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