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| | ==Solution structure of acyl carrier protein LipD from Actinoplanes friuliensis== | | ==Solution structure of acyl carrier protein LipD from Actinoplanes friuliensis== |
| - | <StructureSection load='2n98' size='340' side='right' caption='[[2n98]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''> | + | <StructureSection load='2n98' size='340' side='right'caption='[[2n98]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2n98]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N98 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2N98 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2n98]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Actinoplanes_friuliensis Actinoplanes friuliensis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N98 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N98 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=2n98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n98 OCA], [http://pdbe.org/2n98 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2n98 RCSB], [http://www.ebi.ac.uk/pdbsum/2n98 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2n98 ProSAT]</span></td></tr> | + | </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=2n98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n98 OCA], [https://pdbe.org/2n98 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n98 RCSB], [https://www.ebi.ac.uk/pdbsum/2n98 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n98 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q4H1C9_9ACTN Q4H1C9_9ACTN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Acyl carrier protein|Acyl carrier protein]] | + | *[[Acyl carrier protein 3D structures|Acyl carrier protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ishida, H]] | + | [[Category: Actinoplanes friuliensis]] |
| - | [[Category: Liu, Z]] | + | [[Category: Large Structures]] |
| - | [[Category: Nguyen, L T]] | + | [[Category: Ishida H]] |
| - | [[Category: Paul, S]] | + | [[Category: Liu Z]] |
| - | [[Category: Vogel, H J]] | + | [[Category: Nguyen LT]] |
| - | [[Category: Acyl carrier protein]] | + | [[Category: Paul S]] |
| - | [[Category: Transport protein]] | + | [[Category: Vogel HJ]] |
| Structural highlights
Function
Q4H1C9_9ACTN
Publication Abstract from PubMed
Friulimicin is a cyclic lipodecapeptide antibiotic that is produced by Actinoplanes friuliensis. Similar to the related lipopeptide drug daptomycin, the peptide skeleton of friulimicin is synthesized by a large multienzyme nonribosomal peptide synthetase (NRPS) system. The LipD protein plays a major role in the acylation reaction of friulimicin. The attachment of the fatty acid group promotes its antibiotic activity. Phylogenetic analysis reveals that LipD is most closely related to other freestanding acyl carrier proteins (ACPs), for which the genes are located near to NRPS gene clusters. Here, we report that the solution NMR structure of apo-LipD is very similar to other four-helix bundle forming ACPs from fatty acid synthase (FAS), polyketide synthase, and NRPS systems. By recording NMR dynamics data, we found that the backbone motions in holo-LipD are more restricted than in apo-LipD due to the attachment of phosphopantetheine moiety. This enhanced stability of holo-LipD was also observed in differential scanning calorimetry experiments. Furthermore, we demonstrate that, unlike several other ACPs, the folding of LipD does not depend on the presence of divalent cations, although the presence of Mg2+ or Ca2+ can increase the protein stability. We propose that small structural rearrangements in the tertiary structure of holo-LipD which lead to the enhanced stability are important for the cognate enzyme recognition for the acylation reaction. Our results also highlight the different surface charges of LipD and FAS-ACP from A. friuliensis that would allow the acyl-CoA ligase to interact preferentially with the LipD instead of binding to the FAS-ACP.
Structural and dynamic characterization of a freestanding acyl carrier protein involved in the biosynthesis of cyclic lipopeptide antibiotics.,Paul S, Ishida H, Nguyen LT, Liu Z, Vogel HJ Protein Sci. 2017 Feb 10. doi: 10.1002/pro.3138. PMID:28187530[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Paul S, Ishida H, Nguyen LT, Liu Z, Vogel HJ. Structural and dynamic characterization of a freestanding acyl carrier protein involved in the biosynthesis of cyclic lipopeptide antibiotics. Protein Sci. 2017 Feb 10. doi: 10.1002/pro.3138. PMID:28187530 doi:http://dx.doi.org/10.1002/pro.3138
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