4q86

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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4q86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q86 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4q86 RCSB], [http://www.ebi.ac.uk/pdbsum/4q86 PDBsum]</span></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4q86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q86 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4q86 RCSB], [http://www.ebi.ac.uk/pdbsum/4q86 PDBsum]</span></td></tr>
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== Publication Abstract from PubMed ==
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Despite intensive research, the cyclodehydratase responsible for azoline biogenesis in thiazole/oxazole-modified microcin (TOMM) natural products remains enigmatic. The collaboration of two proteins, C and D, is required for cyclodehydration. The C protein is homologous to E1 ubiquitin-activating enzymes, whereas the D protein is within the YcaO superfamily. Recent studies have demonstrated that TOMM YcaOs phosphorylate amide carbonyl oxygens to facilitate azoline formation. Here we report the X-ray crystal structure of an uncharacterized YcaO from Escherichia coli (Ec-YcaO). Ec-YcaO harbors an unprecedented fold and ATP-binding motif. This motif is conserved among TOMM YcaOs and is required for cyclodehydration. Furthermore, we demonstrate that the C protein regulates substrate binding and catalysis and that the proline-rich C terminus of the D protein is involved in C protein recognition and catalysis. This study identifies the YcaO active site and paves the way for the characterization of the numerous YcaO domains not associated with TOMM biosynthesis.
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Discovery of a new ATP-binding motif involved in peptidic azoline biosynthesis.,Dunbar KL, Chekan JR, Cox CL, Burkhart BJ, Nair SK, Mitchell DA Nat Chem Biol. 2014 Aug 17. doi: 10.1038/nchembio.1608. PMID:25129028<ref>PMID:25129028</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
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<references/>
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Revision as of 02:59, 4 September 2014

YcaO with AMP Bound

4q86, resolution 2.25Å

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