6ww1

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Current revision (14:38, 18 October 2023) (edit) (undo)
 
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==Crystal structure of the LmFPPS mutant E97Y==
==Crystal structure of the LmFPPS mutant E97Y==
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<StructureSection load='6ww1' size='340' side='right'caption='[[6ww1]]' scene=''>
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<StructureSection load='6ww1' size='340' side='right'caption='[[6ww1]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6WW1 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6WW1 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6ww1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Leishmania_major Leishmania major]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6WW1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6WW1 FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6ww1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ww1 OCA], [http://pdbe.org/6ww1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ww1 RCSB], [http://www.ebi.ac.uk/pdbsum/6ww1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ww1 ProSAT]</span></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]] 2.05&#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=476:3-BUTYL-1-(2,2-DIPHOSPHONOETHYL)PYRIDINIUM'>476</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=IPR:ISOPENTYL+PYROPHOSPHATE'>IPR</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=6ww1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ww1 OCA], [https://pdbe.org/6ww1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ww1 RCSB], [https://www.ebi.ac.uk/pdbsum/6ww1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ww1 ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q4QBL1_LEIMA Q4QBL1_LEIMA]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Farnesyl diphosphate synthase (FPPS) is an isoprenoid chain elongation enzyme that catalyzes the sequential condensation of dimethylallyl diphosphate (C5) with isopentenyl diphosphate (IPP; C5) and the resulting geranyl diphosphate (GPP; C10) with another molecule of IPP, eventually producing farnesyl diphosphate (FPP; C15), which is a precursor for the biosynthesis of a vast majority of isoprenoids. Previous studies of FPPS have highlighted the importance of the structure around the hydrophobic chain elongation path in determining product specificity. To investigate what structural features define the final chain length of the product in FPPS from Leishmania major, we designed and expressed six mutants of LmFPPS by replacing small amino acids around the binding pocket with bulky residues. Using enzymatic assays, binding kinetics, and crystallographic studies, we analyzed the effects of these mutations on the activity and product specificity of FPPS. Our results revealed that replacement of Thr-164 with tryptophan and phenylalanine completely abolished the activity of FPPS. Intriguingly, the T164Y substitution displayed dual product specificity and produced a mixture GPP and FPP as final products, with an activity for FPP synthesis that was lower than that of the wild-type enzyme. These data indicate that Thr-164 is a potential regulator of product specificity.
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Identifying Structural Determinants of Product Specificity in Leishmania major Farnesyl Diphosphate Synthase.,Maheshwari S, Kim YS, Aripirala S, Murphy M, Amzel LM, Gabelli SB Biochemistry. 2020 Jul 12. doi: 10.1021/acs.biochem.0c00432. PMID:32584028<ref>PMID:32584028</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 6ww1" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Farnesyl diphosphate synthase 3D structures|Farnesyl diphosphate synthase 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: Leishmania major]]
[[Category: Gabelli SB]]
[[Category: Gabelli SB]]
[[Category: Kim YS]]
[[Category: Kim YS]]
[[Category: Maheshwari S]]
[[Category: Maheshwari S]]

Current revision

Crystal structure of the LmFPPS mutant E97Y

PDB ID 6ww1

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