View source for 6slk


==Diaminobutyrate acetyltransferase EctA from Paenibacillus lautus==
<StructureSection load='6slk' size='340' side='right'caption='[[6slk]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6slk]] is a 3 chain structure with sequence from [https://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=6SLK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SLK FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ectA, GYMC10_5665 ([https://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'>[https://en.wikipedia.org/wiki/Diaminobutyrate_acetyltransferase Diaminobutyrate acetyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.178 2.3.1.178] </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=6slk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6slk OCA], [https://pdbe.org/6slk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6slk RCSB], [https://www.ebi.ac.uk/pdbsum/6slk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6slk ProSAT]</span></td></tr>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/D3EKC1_GEOS4 D3EKC1_GEOS4]] Catalyzes the acetylation of L-2,4-diaminobutyrate (DABA) to gamma-N-acetyl-alpha,gamma-diaminobutyric acid (ADABA) with acetyl coenzyme A.[ARBA:ARBA00003741][RuleBase:RU365045] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Ectoine is a solute compatible with the physiologies of both prokaryotic and eukaryotic cells and is widely synthesized by bacteria as an osmotic stress protectant. Because it preserves functional attributes of proteins and macromolecular complexes, it is considered a chemical chaperone and has found numerous practical applications. However, the mechanism of its biosynthesis is incompletely understood. The second step in ectoine biosynthesis is catalyzed by L-2,4-diaminobutyrate acetyltransferase (EctA; EC 2.3.1.178), which transfers the acetyl group from acetyl CoA to EctB-formed L-2,4-diaminobutyrate (DAB), yielding N-gamma-acetyl-L-2,4-diaminobutyrate (N-gamma-ADABA), the substrate of ectoine synthase (EctC). Here, we report the biochemical and structural characterization of the EctA enzyme from the thermotolerant bacterium Paenibacillus lautus (Pl). We found that (Pl)EctA forms a homodimer whose enzyme activity is highly regiospecific by producing N-gamma-ADABA but not the ectoine catabolic intermediate N-alpha-ADABA. High-resolution crystal structures of (Pl)EctA (at 1.2-2.2 A resolution) for (i) its apo form, (ii) in complex with CoA, (iii) in complex with DAB, (iv) in complex with both with CoA and DAB, and (v) in the presence of the product N-gamma-ADABA were obtained. To pinpoint residues involved in DAB binding, we probed the structure-function relationship of (Pl)EctA by site-directed mutagenesis. Phylogenomics shows that EctA-type proteins from both Bacteria and Archaea are evolutionarily highly conserved, including catalytically important residues. Collectively, our biochemical and structural findings yielded detailed insights into the catalytic core of the EctA enzyme that laid the foundation for unraveling its reaction mechanism.

The architecture of the diaminobutyrate acetyltransferase active site provides mechanistic insight into the biosynthesis of the chemical chaperone ectoine.,Richter AA, Kobus S, Czech L, Hoeppner A, Zarzycki J, Erb TJ, Lauterbach L, Dickschat JS, Bremer E, Smits SHJ J Biol Chem. 2020 Jan 22. pii: RA119.011277. doi: 10.1074/jbc.RA119.011277. PMID:31969391<ref>PMID:31969391</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6slk" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus lautus batchelor 1919]]
[[Category: Diaminobutyrate acetyltransferase]]
[[Category: Large Structures]]
[[Category: Bremer, E]]
[[Category: Czech, L]]
[[Category: Hoeppner, A]]
[[Category: Kobus, S]]
[[Category: Richter, A A]]
[[Category: Smits, S H.J]]
[[Category: 4-diaminobutyrate acetyltransferase]]
[[Category: Acetyl coenzyme some]]
[[Category: Acetylation]]
[[Category: Chemical chaperone]]
[[Category: L-2]]
[[Category: Stress response]]
[[Category: Transferase]]