5egf
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | The | + | ==The crystal structure of SeMet-CT== |
| + | <StructureSection load='5egf' size='340' side='right'caption='[[5egf]], [[Resolution|resolution]] 2.29Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5egf]] 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=5EGF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EGF 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]] 2.29Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=5egf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5egf OCA], [https://pdbe.org/5egf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5egf RCSB], [https://www.ebi.ac.uk/pdbsum/5egf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5egf 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5egf" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Penicillium aethiopicum]] | ||
| + | [[Category: Tang Y]] | ||
| + | [[Category: Zhang JR]] | ||
| + | [[Category: Zhou JH]] | ||
Current revision
The crystal structure of SeMet-CT
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