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| | ==NMR solution structure of meACP== | | ==NMR solution structure of meACP== |
| - | <StructureSection load='2l9f' size='340' side='right' caption='[[2l9f]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | + | <StructureSection load='2l9f' size='340' side='right'caption='[[2l9f]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2l9f]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_15837 Atcc 15837]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L9F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L9F FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2l9f]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Micromonospora_echinospora Micromonospora echinospora]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L9F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L9F FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2l9f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l9f OCA], [http://pdbe.org/2l9f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2l9f RCSB], [http://www.ebi.ac.uk/pdbsum/2l9f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2l9f ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2l9f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l9f OCA], [https://pdbe.org/2l9f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l9f RCSB], [https://www.ebi.ac.uk/pdbsum/2l9f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l9f ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8KNG1_MICEC Q8KNG1_MICEC] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 15837]] | + | [[Category: Large Structures]] |
| - | [[Category: Ho, C L]]
| + | |
| - | [[Category: Kong, R]]
| + | |
| - | [[Category: Liang, Z X]]
| + | |
| - | [[Category: Lim, J]]
| + | |
| - | [[Category: Murugan, E]]
| + | |
| - | [[Category: Yang, D]]
| + | |
| - | [[Category: Acyl carrier protein]]
| + | |
| | [[Category: Micromonospora echinospora]] | | [[Category: Micromonospora echinospora]] |
| - | [[Category: Transferase]] | + | [[Category: Ho CL]] |
| | + | [[Category: Kong R]] |
| | + | [[Category: Liang ZX]] |
| | + | [[Category: Lim J]] |
| | + | [[Category: Murugan E]] |
| | + | [[Category: Yang D]] |
| Structural highlights
Function
Q8KNG1_MICEC
Publication Abstract from PubMed
Biosynthesis of the enediyne natural product calicheamicins gamma(1) (I) in Micromonospora echinospora ssp. calichensis is initiated by the iterative polyketide synthase (PKS) CalE8. Recent studies showed that CalE8 produces highly conjugated polyenes as potential biosynthetic intermediates and thus belongs to a family of highly-reducing (HR) type I iterative PKSs. We have determined the NMR structure of the ACP domain (meACP) of CalE8, which represents the first structure of a HR type I iterative PKS ACP domain. Featured by a distinct hydrophobic patch and a glutamate-residue rich acidic patch, meACP adopts a twisted three-helix bundle structure rather than the canonical four-helix bundle structure. The so-called 'recognition helix' (alpha2) of meACP is less negatively charged than the typical type II ACPs. Although loop-2 exhibits greater conformational mobility than other regions of the protein with a missing short helix that can be observed in most ACPs, two bulky non-polar residues (Met(992), Phe(996)) from loop-2 packed against the hydrophobic protein core seem to restrict large movement of the loop and impede the opening of the hydrophobic pocket for sequestering the acyl chains. NMR studies of the hydroxybutyryl- and octanoyl-meACP confirm that meACP is unable to sequester the hydrophobic chains in a well-defined central cavity. Instead, meACP seems to interact with the octanoyl tail through a distinct hydrophobic patch without involving large conformational change of loop-2. NMR titration study of the interaction between meACP and the cognate thioesterase partner CalE7 further suggests that their interaction is likely through the binding of CalE7 to the meACP-tethered polyene moiety rather than direct specific protein-protein interaction.
Solution structures of the acyl carrier protein domain from the highly reducing type I iterative polyketide synthase CalE8.,Lim J, Kong R, Murugan E, Ho CL, Liang ZX, Yang D PLoS One. 2011;6(6):e20549. Epub 2011 Jun 2. PMID:21674045[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lim J, Kong R, Murugan E, Ho CL, Liang ZX, Yang D. Solution structures of the acyl carrier protein domain from the highly reducing type I iterative polyketide synthase CalE8. PLoS One. 2011;6(6):e20549. Epub 2011 Jun 2. PMID:21674045 doi:10.1371/journal.pone.0020549
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