6v04: Difference between revisions

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6v04 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6v04 OCA], [https://pdbe.org/6v04 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6v04 RCSB], [https://www.ebi.ac.uk/pdbsum/6v04 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6v04 ProSAT]</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=6v04 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6v04 OCA], [https://pdbe.org/6v04 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6v04 RCSB], [https://www.ebi.ac.uk/pdbsum/6v04 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6v04 ProSAT]</span></td></tr>
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== Publication Abstract from PubMed ==
The 1.5 A resolution crystal structure of DynU16, a protein identified in the dynemicin-biosynthetic gene cluster, is reported. The structure adopts a di-domain helix-grip fold with a uniquely positioned open cavity connecting the domains. The elongated dimensions of the cavity appear to be compatible with the geometry of a linear polyene, suggesting the involvement of DynU16 in the upstream steps of dynemicin biosynthesis.
Structural characterization of DynU16, a START/Bet v1-like protein involved in dynemicin biosynthesis.,Alvarado SK, Miller MD, Bhardwaj M, Thorson JS, Van Lanen SG, Phillips GN Jr Acta Crystallogr F Struct Biol Commun. 2021 Oct 1;77(Pt 10):328-333. doi:, 10.1107/S2053230X21008943. Epub 2021 Sep 21. PMID:34605436<ref>PMID:34605436</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6v04" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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