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| | <StructureSection load='5onm' size='340' side='right'caption='[[5onm]], [[Resolution|resolution]] 1.52Å' scene=''> | | <StructureSection load='5onm' size='340' side='right'caption='[[5onm]], [[Resolution|resolution]] 1.52Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5onm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_lautus"_batchelor_1919 "bacillus lautus" batchelor 1919]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ONM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ONM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5onm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Paenibacillus_lautus Paenibacillus lautus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ONM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ONM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.52Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ectC, BK123_26285 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1401 "Bacillus lautus" Batchelor 1919])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ectoine_synthase Ectoine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.108 4.2.1.108] </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=5onm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5onm OCA], [https://pdbe.org/5onm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5onm RCSB], [https://www.ebi.ac.uk/pdbsum/5onm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5onm ProSAT]</span></td></tr> |
| - | <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=5onm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5onm OCA], [http://pdbe.org/5onm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5onm RCSB], [http://www.ebi.ac.uk/pdbsum/5onm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5onm ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/A0A1R1AV52_PAELA A0A1R1AV52_PAELA]] Catalyzes the circularization of gamma-N-acetyl-alpha,gamma-diaminobutyric acid (ADABA) to ectoine (1,4,5,6-tetrahydro-2-methyl-4-pyrimidine carboxylic acid), which is an excellent osmoprotectant.[HAMAP-Rule:MF_01255] | + | [https://www.uniprot.org/uniprot/A0A1R1AV52_PAELA A0A1R1AV52_PAELA] Catalyzes the circularization of gamma-N-acetyl-alpha,gamma-diaminobutyric acid (ADABA) to ectoine (1,4,5,6-tetrahydro-2-methyl-4-pyrimidine carboxylic acid), which is an excellent osmoprotectant.[HAMAP-Rule:MF_01255] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus lautus batchelor 1919]] | |
| - | [[Category: Ectoine synthase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bremer, E]] | + | [[Category: Paenibacillus lautus]] |
| - | [[Category: Ectoine]] | + | [[Category: Bremer E]] |
| - | [[Category: Metal binding protein]]
| + | |
| - | [[Category: Osmolyte]]
| + | |
| - | [[Category: Synthase]]
| + | |
| Structural highlights
Function
A0A1R1AV52_PAELA Catalyzes the circularization of gamma-N-acetyl-alpha,gamma-diaminobutyric acid (ADABA) to ectoine (1,4,5,6-tetrahydro-2-methyl-4-pyrimidine carboxylic acid), which is an excellent osmoprotectant.[HAMAP-Rule:MF_01255]
Publication Abstract from PubMed
Ectoine synthase (EctC) is the signature enzyme for the production of ectoine, a compatible solute and chemical chaperone widely synthesized by bacteria as a cellular defense against the detrimental effects of osmotic stress. EctC catalyzes the last step in ectoine synthesis through cyclo-condensation of the EctA-formed substrate N-gamma-acetyl-L-2,4-diaminobutyric acid via a water elimination reaction. We have biochemically and structurally characterized the EctC enzyme from the thermo-tolerant bacterium Paenibacillus lautus (Pl). EctC is a member of the cupin superfamily and forms dimers, both in solution and in crystals. We obtained high-resolution crystal structures of the (Pl)EctC protein in forms that contain (i) the catalytically important iron, (ii) iron and the substrate N-gamma-acetyl-L-2,4-diaminobutyric acid, and (iii) iron and the enzyme reaction product ectoine. These crystal structures lay the framework for a proposal for the EctC-mediated water-elimination reaction mechanism. Residues involved in coordinating the metal, the substrate, or the product within the active site of ectoine synthase are highly conserved among a large group of EctC-type proteins. Collectively, the biochemical, mutational, and structural data reported here yielded detailed insight into the structure-function relationship of the (Pl)EctC enzyme and are relevant for a deeper understanding of the ectoine synthase family as a whole.
Illuminating the catalytic core of ectoine synthase through structural and biochemical analysis.,Czech L, Hoppner A, Kobus S, Seubert A, Riclea R, Dickschat JS, Heider J, Smits SHJ, Bremer E Sci Rep. 2019 Jan 23;9(1):364. doi: 10.1038/s41598-018-36247-w. PMID:30674920[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Czech L, Hoppner A, Kobus S, Seubert A, Riclea R, Dickschat JS, Heider J, Smits SHJ, Bremer E. Illuminating the catalytic core of ectoine synthase through structural and biochemical analysis. Sci Rep. 2019 Jan 23;9(1):364. doi: 10.1038/s41598-018-36247-w. PMID:30674920 doi:http://dx.doi.org/10.1038/s41598-018-36247-w
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