View source for 2xhg


==Crystal Structure of the Epimerization Domain from the Initiation Module of Tyrocidine Biosynthesis==
<StructureSection load='2xhg' size='340' side='right'caption='[[2xhg]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2xhg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Brevibacillus_brevis Brevibacillus brevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XHG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XHG 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]] 1.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=2xhg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xhg OCA], [https://pdbe.org/2xhg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xhg RCSB], [https://www.ebi.ac.uk/pdbsum/2xhg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xhg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/G1K3P2_BREBE G1K3P2_BREBE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Tyrocidine, a macrocyclic decapeptide from Bacillus brevis, is nonribosomally assembled by a set of multimodular peptide synthetases, which condense two D-amino acids and eight L-amino acids to produce this membrane-disturbing antibiotic. D-Phenylalanine, the first amino acid incorporated into tyrocidine, is catalytically derived from enzyme-bound L-Phe by the C-terminal epimerization (E) domain of tyrocidine synthetase A (TycA). The 1.5 A resolution structure of the cofactor-independent TycA E domain reveals an intimate relationship to the condensation (C) domains of peptide synthetases. In contrast to the latter, the TycA E domain uses an enlarged bridge region to plug the active-site canyon from the acceptor side, whereas at the donor side a latch-like floor loop is suitably extended to accommodate the alphaIII helix of the preceding peptide-carrier domain. Additionally, E domains exclusively harbour a conserved glutamate residue, Glu882, that is opposite the active-site residue His743. This active-site topology implies Glu882 as a candidate acid-base catalyst, whereas His743 stabilizes in the protonated state a transient enolate intermediate of the L&lt;--&gt;D isomerization.

Structure of the epimerization domain of tyrocidine synthetase A.,Samel SA, Czodrowski P, Essen LO Acta Crystallogr D Biol Crystallogr. 2014 May;70(Pt 5):1442-52. doi:, 10.1107/S1399004714004398. Epub 2014 Apr 30. PMID:24816112<ref>PMID:24816112</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2xhg" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Brevibacillus brevis]]
[[Category: Large Structures]]
[[Category: Essen L-O]]
[[Category: Heine A]]
[[Category: Marahiel MA]]
[[Category: Samel S-A]]