View source for 5onn


==Crystal Structure of Ectoine Synthase from P. lautus==
<StructureSection load='5onn' size='340' side='right'caption='[[5onn]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5onn]] 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=5ONN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ONN FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9YT:(2~{S})-4-acetamido-2-azanyl-butanoic+acid'>9YT</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></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=5onn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5onn OCA], [https://pdbe.org/5onn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5onn RCSB], [https://www.ebi.ac.uk/pdbsum/5onn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5onn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A2A5LBI6_PAELA A0A2A5LBI6_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 5onn" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Paenibacillus lautus]]
[[Category: Bremer E]]