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| | <StructureSection load='6c9u' size='340' side='right'caption='[[6c9u]], [[Resolution|resolution]] 2.09Å' scene=''> | | <StructureSection load='6c9u' size='340' side='right'caption='[[6c9u]], [[Resolution|resolution]] 2.09Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6c9u]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_erythreus"_(sic)_waksman_1923 "actinomyces erythreus" (sic) waksman 1923] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6C9U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6C9U FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6c9u]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Saccharopolyspora_erythraea Saccharopolyspora erythraea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6C9U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6C9U FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 2.09Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">eryA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1836 "Actinomyces erythreus" (sic) Waksman 1923])</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=6c9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6c9u OCA], [https://pdbe.org/6c9u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6c9u RCSB], [https://www.ebi.ac.uk/pdbsum/6c9u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6c9u 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/6-deoxyerythronolide-B_synthase 6-deoxyerythronolide-B synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.94 2.3.1.94] </span></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=6c9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6c9u OCA], [http://pdbe.org/6c9u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6c9u RCSB], [http://www.ebi.ac.uk/pdbsum/6c9u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6c9u ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/ERYA2_SACER ERYA2_SACER] |
| | <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== |
| | + | *[[Antibody 3D structures|Antibody 3D structures]] |
| | *[[6-deoxyerythronolide B synthase 3D structures|6-deoxyerythronolide B synthase 3D structures]] | | *[[6-deoxyerythronolide B synthase 3D structures|6-deoxyerythronolide B synthase 3D structures]] |
| | == References == | | == References == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: 6-deoxyerythronolide-B synthase]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Human]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Deis, L N]] | + | [[Category: Saccharopolyspora erythraea]] |
| - | [[Category: Khosla, C]] | + | [[Category: Deis LN]] |
| - | [[Category: Li, X]] | + | [[Category: Khosla C]] |
| - | [[Category: Mathews, I I]] | + | [[Category: Li X]] |
| - | [[Category: 6-deoxyerthronolide b synthase]] | + | [[Category: Mathews II]] |
| - | [[Category: Antibody]]
| + | |
| - | [[Category: Deb]]
| + | |
| - | [[Category: Fab]]
| + | |
| - | [[Category: Phage display]]
| + | |
| - | [[Category: Pk]]
| + | |
| - | [[Category: Polyketide synthase]]
| + | |
| - | [[Category: Transferase-immune system complex]]
| + | |
| Structural highlights
Function
ERYA2_SACER
Publication Abstract from PubMed
Catalytic modules of assembly-line polyketide synthases (PKSs) have previously been observed in two very different conformations-an "extended" architecture and an "arch-shaped" architecture-although the catalytic relevance of neither has been directly established. By the use of a fully human naive antigen-binding fragment (Fab) library, a high-affinity antibody was identified that bound to the extended conformation of a PKS module, as verified by X-ray crystallography and tandem size-exclusion chromatography-small-angle X-ray scattering (SEC-SAXS). Kinetic analysis proved that this antibody-stabilized module conformation was fully competent for catalysis of intermodular polyketide chain translocation as well as intramodular polyketide chain elongation and functional group modification of a growing polyketide chain. Thus, the extended conformation of a PKS module is fully competent for all of its essential catalytic functions.
Structure-Function Analysis of the Extended Conformation of a Polyketide Synthase Module.,Li X, Sevillano N, La Greca F, Deis L, Liu YC, Deller MC, Mathews II, Matsui T, Cane DE, Craik CS, Khosla C J Am Chem Soc. 2018 May 18. doi: 10.1021/jacs.8b02100. PMID:29762030[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Li X, Sevillano N, La Greca F, Deis L, Liu YC, Deller MC, Mathews II, Matsui T, Cane DE, Craik CS, Khosla C. Structure-Function Analysis of the Extended Conformation of a Polyketide Synthase Module. J Am Chem Soc. 2018 May 18. doi: 10.1021/jacs.8b02100. PMID:29762030 doi:http://dx.doi.org/10.1021/jacs.8b02100
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