5ono: Difference between revisions

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==Crystal Structure of Ectoine Synthase from P. lautus==

== Structural highlights ==

<table><tr><td colspan='2'>[[5ono]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ONO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ONO FirstGlance]. <br>

<table><tr><td colspan='2'>[[5ono]] 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=5ONO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ONO FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4CS:(4S)-2-METHYL-1,4,5,6-TETRAHYDROPYRIMIDINE-4-CARBOXYLIC+ACID'>4CS</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5onn|5onn]]</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='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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ono FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ono OCA], [http://pdbe.org/5ono PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ono RCSB], [http://www.ebi.ac.uk/pdbsum/5ono PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ono ProSAT]</span></td></tr>

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== 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]

== 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<ref>PMID:30674920</ref>

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

== References ==

__TOC__

</StructureSection>

[[Category: Bacillus lautus batchelor 1919]]

[[Category: Ectoine synthase]]

[[Category: Bremer, E]]

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@@ Line 1: / Line 1: @@
 ==Crystal Structure of Ectoine Synthase from P. lautus==
-<StructureSection load='5ono' size='340' side='right' caption='[[5ono]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+<StructureSection load='5ono' size='340' side='right'  caption='[[5ono]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5ono]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ONO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ONO FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5ono]] 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=5ONO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ONO FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4CS:(4S)-2-METHYL-1,4,5,6-TETRAHYDROPYRIMIDINE-4-CARBOXYLIC+ACID'>4CS</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5onn|5onn]]</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='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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ono FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ono OCA], [http://pdbe.org/5ono PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ono RCSB], [http://www.ebi.ac.uk/pdbsum/5ono PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ono ProSAT]</span></td></tr>
@@ Line 11: / Line 12: @@
 == 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]
+<div style="background-color:#fffaf0;">
+== 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<ref>PMID:30674920</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 5ono" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>
+[[Category: Bacillus lautus batchelor 1919]]
 [[Category: Ectoine synthase]]
 [[Category: Bremer, E]]