6smd: Difference between revisions

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<StructureSection load='6smd' size='340' side='right'caption='[[6smd]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
<StructureSection load='6smd' size='340' side='right'caption='[[6smd]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6smd]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_29999 Atcc 29999]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SMD OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6SMD FirstGlance]. <br>
<table><tr><td colspan='2'>[[6smd]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Photorhabdus_luminescens Photorhabdus luminescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SMD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SMD FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=4HH:O-[(S)-HYDROXY{[(3R)-3-HYDROXY-2,2-DIMETHYL-4-OXO-4-({3-OXO-3-[(2-SULFANYLETHYL)AMINO]PROPYL}AMINO)BUTYL]OXY}PHOSPHORYL]-L-SERINE'>4HH</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.3&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2g1h|2g1h]], [[6sm6|6sm6]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4HH:O-[(S)-HYDROXY{[(3R)-3-HYDROXY-2,2-DIMETHYL-4-OXO-4-({3-OXO-3-[(2-SULFANYLETHYL)AMINO]PROPYL}AMINO)BUTYL]OXY}PHOSPHORYL]-L-SERINE'>4HH</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">C6H68_21855 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29488 ATCC 29999]), fabD, plu2834 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29488 ATCC 29999])</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=6smd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6smd OCA], [https://pdbe.org/6smd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6smd RCSB], [https://www.ebi.ac.uk/pdbsum/6smd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6smd ProSAT]</span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/[Acyl-carrier-protein]_S-malonyltransferase [Acyl-carrier-protein] S-malonyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.39 2.3.1.39] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6smd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6smd OCA], [http://pdbe.org/6smd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6smd RCSB], [http://www.ebi.ac.uk/pdbsum/6smd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6smd ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A2S8QL96_PHOLU A0A2S8QL96_PHOLU]
<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 29999]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Bode, H]]
[[Category: Photorhabdus luminescens]]
[[Category: Braeuer, A]]
[[Category: Bode H]]
[[Category: Grammbitter, G L.C]]
[[Category: Braeuer A]]
[[Category: Groll, M]]
[[Category: Grammbitter GLC]]
[[Category: Kaila, V R.I]]
[[Category: Groll M]]
[[Category: Ruehl, M]]
[[Category: Kaila VRI]]
[[Category: Schmalhofer, M]]
[[Category: Ruehl M]]
[[Category: Zhou, Q]]
[[Category: Schmalhofer M]]
[[Category: Anthraquinone]]
[[Category: Zhou Q]]
[[Category: Catalysis]]
[[Category: Chain elongation]]
[[Category: Minimal pks system]]
[[Category: Natural product biosynthesis]]
[[Category: Polyketide]]
[[Category: Protein binding]]

Latest revision as of 15:44, 24 January 2024

PlMCAT:AntF (holo): type II PKS acyl-carrier protein in complex with its malonyl-transacylasePlMCAT:AntF (holo): type II PKS acyl-carrier protein in complex with its malonyl-transacylase

Structural highlights

6smd is a 3 chain structure with sequence from Photorhabdus luminescens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.3Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

A0A2S8QL96_PHOLU

Publication Abstract from PubMed

Type II polyketide synthases (PKSs) are multi-enzyme complexes that produce secondary metabolites of medical relevance. Chemical backbones of such polyketides are produced by minimal PKS systems that consist of a malonyl transacylase, an acyl carrier protein and an alpha/beta heterodimeric ketosynthase. Here, we present X-ray structures of all ternary complexes that constitute the minimal PKS system for anthraquinone biosynthesis in Photorhabdus luminescens. In addition, we characterize this invariable core using molecular simulations, mutagenesis experiments and functional assays. We show that malonylation of the acyl carrier protein is accompanied by major structural rearrangements in the transacylase. Principles of an ongoing chain elongation are derived from the ternary complex with a hexaketide covalently linking the heterodimeric ketosynthase with the acyl carrier protein. Our results for the minimal PKS system provide mechanistic understanding of PKSs and a fundamental basis for engineering PKS pathways for future applications.

Structural snapshots of the minimal PKS system responsible for octaketide biosynthesis.,Brauer A, Zhou Q, Grammbitter GLC, Schmalhofer M, Ruhl M, Kaila VRI, Bode HB, Groll M Nat Chem. 2020 Aug;12(8):755-763. doi: 10.1038/s41557-020-0491-7. Epub 2020 Jul, 6. PMID:32632186[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Brauer A, Zhou Q, Grammbitter GLC, Schmalhofer M, Ruhl M, Kaila VRI, Bode HB, Groll M. Structural snapshots of the minimal PKS system responsible for octaketide biosynthesis. Nat Chem. 2020 Aug;12(8):755-763. doi: 10.1038/s41557-020-0491-7. Epub 2020 Jul, 6. PMID:32632186 doi:http://dx.doi.org/10.1038/s41557-020-0491-7

6smd, resolution 3.30Å

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OCA