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| | <StructureSection load='6m01' size='340' side='right'caption='[[6m01]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='6m01' size='340' side='right'caption='[[6m01]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6m01]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Dsm_41855 Dsm 41855]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6M01 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6M01 FirstGlance]. <br> | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6M01 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6M01 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9EF:N-[2-(acetylamino)ethyl]-N~3~-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alaninamide'>9EF</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hitB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=159449 DSM 41855]), hitD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=159449 DSM 41855])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9EF:N-[2-(acetylamino)ethyl]-N~3~-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alaninamide'>9EF</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=6m01 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6m01 OCA], [http://pdbe.org/6m01 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6m01 RCSB], [http://www.ebi.ac.uk/pdbsum/6m01 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6m01 ProSAT]</span></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=6m01 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6m01 OCA], [https://pdbe.org/6m01 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6m01 RCSB], [https://www.ebi.ac.uk/pdbsum/6m01 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6m01 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Dsm 41855]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Eguchi, T]] | + | [[Category: Eguchi T]] |
| - | [[Category: Kudo, F]] | + | [[Category: Kudo F]] |
| - | [[Category: Kurihara, S]] | + | [[Category: Kurihara S]] |
| - | [[Category: Miyanaga, A]] | + | [[Category: Miyanaga A]] |
| - | [[Category: Adenylation]]
| + | |
| - | [[Category: Atp binding]]
| + | |
| - | [[Category: Carrier protein]]
| + | |
| - | [[Category: Hitachimycin]]
| + | |
| - | [[Category: Ligase]]
| + | |
| - | [[Category: Polyketide biosynthesis]]
| + | |
| Structural highlights
Publication Abstract from PubMed
Adenylation domains (A-domains) are responsible for selective incorporation of carboxylic acid substrates in the biosynthesis of various natural products. Each A-domain must recognize a cognate carrier protein (CP) for functional substrate transfer. The transient interactions between an A-domain and CP have been investigated by using acyl vinylsulfonamide adenosine inhibitors as probes to determine the structures of several A-domain-CP complexes. However, this strategy requires a specific vinylsulfonamide inhibitor that contains an acyl group corresponding to the substrate specificity of a target A-domain in every case. Here, we report an alternative strategy for structural characterization of A-domain-CP complexes. We used a bromoacetamide pantetheine cross-linking probe in combination with a Cys mutation to trap the standalone A-domain-CP complex involved in macrolactam polyketide biosynthesis through a covalent linkage, allowing the determination of the complex structure. This strategy facilitates the structural determination of A-domain-CP complexes.
Structural Characterization of Complex of Adenylation Domain and Carrier Protein by Using Pantetheine Cross-Linking Probe.,Miyanaga A, Kurihara S, Chisuga T, Kudo F, Eguchi T ACS Chem Biol. 2020 Jul 7. doi: 10.1021/acschembio.0c00403. PMID:32608966[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Miyanaga A, Kurihara S, Chisuga T, Kudo F, Eguchi T. Structural Characterization of Complex of Adenylation Domain and Carrier Protein by Using Pantetheine Cross-Linking Probe. ACS Chem Biol. 2020 Jul 7. doi: 10.1021/acschembio.0c00403. PMID:32608966 doi:http://dx.doi.org/10.1021/acschembio.0c00403
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