2qap

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[[Image:2qap.png|left|200px]]
 
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{{STRUCTURE_2qap| PDB=2qap | SCENE= }}
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==Fructose-1,6-bisphosphate aldolase from Leishmania mexicana==
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<StructureSection load='2qap' size='340' side='right'caption='[[2qap]], [[Resolution|resolution]] 1.59&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2qap]] is a 4 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=2QAP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QAP 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]] 1.59&#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=2qap FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qap OCA], [https://pdbe.org/2qap PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qap RCSB], [https://www.ebi.ac.uk/pdbsum/2qap PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qap ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q9U5N6_LEIME Q9U5N6_LEIME]
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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/qa/2qap_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=2qap 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 crystal structures of Leishmania mexicana fructose-1,6-bis(phosphate) aldolase in complex with substrate and competitive inhibitor, mannitol-1,6-bis(phosphate), were solved to 2.2 A resolution. Crystallographic analysis revealed a Schiff base intermediate trapped in the native structure complexed with substrate while the inhibitor was trapped in a conformation mimicking the carbinolamine intermediate. Binding modes corroborated previous structures reported for rabbit muscle aldolase. Amino acid substitution of Gly-312 to Ala, adjacent to the P1-phosphate binding site and unique to trypanosomatids, did not perturb ligand binding in the active site. Ligand attachment ordered amino acid residues 359-367 of the C-terminal region (353-373) that was disordered beyond Asp-358 in the unbound structure, revealing a novel recruitment mechanism of this region by aldolases. C-Terminal peptide ordering is triggered by P1-phosphate binding that induces conformational changes whereby C-terminal Leu-364 contacts P1-phosphate binding residue Arg-313. C-Terminal region capture synergizes additional interactions with subunit surface residues, not perturbed by P1-phosphate binding, and stabilizes C-terminal attachment. Amino acid residues that participate in the capturing interaction are conserved among class I aldolases, indicating a general recruitment mechanism whereby C-terminal capture facilitates active site interactions in subsequent catalytic steps. Recruitment accelerates the enzymatic reaction by using binding energy to reduce configurational entropy during catalysis thereby localizing the conserved C-terminus tyrosine, which mediates proton transfer, proximal to the active site enamine.
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===Fructose-1,6-bisphosphate aldolase from Leishmania mexicana===
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Carboxy-terminus recruitment induced by substrate binding in eukaryotic fructose bis-phosphate aldolases.,Lafrance-Vanasse J, Sygusch J Biochemistry. 2007 Aug 21;46(33):9533-40. Epub 2007 Jul 28. PMID:17661446<ref>PMID:17661446</ref>
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{{ABSTRACT_PUBMED_17661446}}
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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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==About this Structure==
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<div class="pdbe-citations 2qap" style="background-color:#fffaf0;"></div>
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[[2qap]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Leishmania_mexicana Leishmania mexicana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QAP OCA].
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==See Also==
==See Also==
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*[[Aldolase|Aldolase]]
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*[[Aldolase 3D structures|Aldolase 3D structures]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:017661446</ref><references group="xtra"/>
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__TOC__
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[[Category: Fructose-bisphosphate aldolase]]
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Leishmania mexicana]]
[[Category: Leishmania mexicana]]
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[[Category: Lafrance-Vanasse, J.]]
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[[Category: Lafrance-Vanasse J]]
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[[Category: Sygusch, J.]]
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[[Category: Sygusch J]]
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[[Category: 6-bisphosphate]]
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[[Category: Aldolase]]
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[[Category: Beta barrel]]
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[[Category: C-teminal tail]]
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[[Category: Fructose-1]]
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[[Category: Leishmania]]
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[[Category: Lyase]]
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Current revision

Fructose-1,6-bisphosphate aldolase from Leishmania mexicana

PDB ID 2qap

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