5dlk: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Unreleased structure'''
-The entry 5dlk is ON HOLD  until Paper Publication
+==The crystal structure of CT mutant==
+<StructureSection load='5dlk' size='340' side='right'caption='[[5dlk]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5dlk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Penicillium_aethiopicum Penicillium aethiopicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DLK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DLK 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]] 1.8&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=5dlk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dlk OCA], [https://pdbe.org/5dlk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dlk RCSB], [https://www.ebi.ac.uk/pdbsum/5dlk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dlk ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/F1CWE4_PENAE F1CWE4_PENAE]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Nonribosomal peptide synthetases (NRPSs) in fungi biosynthesize important pharmaceutical compounds, including penicillin, cyclosporine and echinocandin. To understand the fungal strategy of forging the macrocyclic peptide linkage, we determined the crystal structures of the terminal condensation-like (CT) domain and the holo thiolation (T)-CT complex of Penicillium aethiopicum TqaA. The first, to our knowledge, structural depiction of the terminal module in a fungal NRPS provides a molecular blueprint for generating new macrocyclic peptide natural products.
-Authors: Zhang, J.R., Tang, Y., Zhou, J.H.
+Structural basis of nonribosomal peptide macrocyclization in fungi.,Zhang J, Liu N, Cacho RA, Gong Z, Liu Z, Qin W, Tang C, Tang Y, Zhou J Nat Chem Biol. 2016 Dec;12(12):1001-1003. doi: 10.1038/nchembio.2202. Epub 2016, Oct 17. PMID:27748753<ref>PMID:27748753</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Zhang, J.R]]
+<div class="pdbe-citations 5dlk" style="background-color:#fffaf0;"></div>
-[[Category: Zhou, J.H]]
+== References ==
-[[Category: Tang, Y]]
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Penicillium aethiopicum]]
+[[Category: Tang Y]]
+[[Category: Zhang JR]]
+[[Category: Zhou JH]]