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4qnk

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<StructureSection load='4qnk' size='340' side='right'caption='[[4qnk]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
<StructureSection load='4qnk' size='340' side='right'caption='[[4qnk]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4qnk]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QNK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QNK FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4qnk]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QNK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QNK FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 1.75&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4mu0|4mu0]], [[4mu1|4mu1]], [[4mu3|4mu3]], [[4mu4|4mu4]], [[4qnj|4qnj]]</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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">At4g14910, dl3495c, HISN5B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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=4qnk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qnk OCA], [https://pdbe.org/4qnk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qnk RCSB], [https://www.ebi.ac.uk/pdbsum/4qnk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qnk ProSAT]</span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Imidazoleglycerol-phosphate_dehydratase Imidazoleglycerol-phosphate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.19 4.2.1.19] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4qnk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qnk OCA], [http://pdbe.org/4qnk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qnk RCSB], [http://www.ebi.ac.uk/pdbsum/4qnk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qnk ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/HIS5B_ARATH HIS5B_ARATH]
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Imidazoleglycerol-phosphate dehydratase (IGPD) catalyzes the Mn(II)-dependent dehydration of imidazoleglycerol phosphate (IGP) to 3-(1H-imidazol-4-yl)-2-oxopropyl dihydrogen phosphate during biosynthesis of histidine. As part of a program of herbicide design, we have determined a series of high-resolution crystal structures of an inactive mutant of IGPD2 from Arabidopsis thaliana in complex with IGP. The structures represent snapshots of the enzyme trapped at different stages of the catalytic cycle and show how substrate binding triggers a switch in the coordination state of an active site Mn(II) between six- and five-coordinate species. This switch is critical to prime the active site for catalysis, by facilitating the formation of a high-energy imidazolate intermediate. This work not only provides evidence for the molecular processes that dominate catalysis in IGPD, but also describes how the manipulation of metal coordination can be linked to discrete steps in catalysis, demonstrating one way that metalloenzymes exploit the unique properties of metal ions to diversify their chemistry.
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Crystal Structures Reveal that the Reaction Mechanism of Imidazoleglycerol-Phosphate Dehydratase Is Controlled by Switching Mn(II) Coordination.,Bisson C, Britton KL, Sedelnikova SE, Rodgers HF, Eadsforth TC, Viner RC, Hawkes TR, Baker PJ, Rice DW Structure. 2015 Jul 7;23(7):1236-45. doi: 10.1016/j.str.2015.05.012. Epub 2015, Jun 18. PMID:26095028<ref>PMID:26095028</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 4qnk" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Arath]]
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[[Category: Arabidopsis thaliana]]
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[[Category: Imidazoleglycerol-phosphate dehydratase]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Baker, P J]]
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[[Category: Baker PJ]]
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[[Category: Bisson, C]]
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[[Category: Bisson C]]
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[[Category: Britton, K L]]
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[[Category: Britton KL]]
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[[Category: Eadsforth, T C]]
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[[Category: Eadsforth TC]]
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[[Category: Hawkes, T R]]
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[[Category: Hawkes TR]]
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[[Category: Rice, D W]]
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[[Category: Rice DW]]
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[[Category: Rodgers, H F]]
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[[Category: Rodgers HF]]
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[[Category: Sedelnikova, S E]]
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[[Category: Sedelnikova SE]]
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[[Category: Viner, R]]
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[[Category: Viner R]]
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[[Category: Chloroplastic]]
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[[Category: Histidine biosynthesis]]
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[[Category: Hydro-lyase]]
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[[Category: Lyase]]
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[[Category: Manganese binding]]
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Current revision

The structure of wt A. thaliana IGPD2 in complex with Mn2+ and phosphate

PDB ID 4qnk

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