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| | <StructureSection load='3rgi' size='340' side='right'caption='[[3rgi]], [[Resolution|resolution]] 1.51Å' scene=''> | | <StructureSection load='3rgi' size='340' side='right'caption='[[3rgi]], [[Resolution|resolution]] 1.51Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3rgi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"polyangium_compositum"_thaxter_1904 "polyangium compositum" thaxter 1904]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RGI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RGI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3rgi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sorangium_cellulosum Sorangium cellulosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RGI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RGI FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3rgj|3rgj]]</div></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]] 1.51Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dszD, disD ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=56 "Polyangium compositum" Thaxter 1904])</td></tr>
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| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/[Acyl-carrier-protein]_S-malonyltransferase [Acyl-carrier-protein] S-malonyltransferase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=3rgi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rgi OCA], [https://pdbe.org/3rgi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rgi RCSB], [https://www.ebi.ac.uk/pdbsum/3rgi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rgi 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=3rgi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rgi OCA], [https://pdbe.org/3rgi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rgi RCSB], [https://www.ebi.ac.uk/pdbsum/3rgi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rgi ProSAT]</span></td></tr> |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/Q4U443_SORCE Q4U443_SORCE] |
| - | The 1.51 A resolution X-ray crystal structure of the trans-acyltransferase (AT) from the "AT-less" disorazole synthase (DSZS) and that of its acetate complex at 1.35 A resolution are reported. Separately, comprehensive alanine-scanning mutagenesis of one of its acyl carrier protein substrates (ACP1 from DSZS) led to the identification of a conserved Asp45 residue on the ACP, which contributes to the substrate specificity of this unusual enzyme. Together, these experimental findings were used to derive a model for the selective association of the DSZS AT and its ACP substrate. With a goal of structurally characterizing the AT-ACP interface, a strategy was developed for covalently cross-linking the active site Ser --> Cys mutant of the DSZS AT to its ACP substrate and for purifying the resulting AT-ACP complex to homogeneity. The S86C DSZS AT mutant was found to be functional, albeit with a transacylation efficiency 200-fold lower than that of its wild-type counterpart. Our findings provide new insights as well as new opportunities for high-resolution analysis of an important protein-protein interface in polyketide synthases.
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| - | | + | |
| - | Structure and Mechanism of the trans-Acting Acyltransferase from the Disorazole Synthase.,Wong FT, Jin X, Mathews II, Cane DE, Khosla C Biochemistry. 2011 Jul 5. PMID:21707057<ref>PMID:21707057</ref>
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| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 3rgi" style="background-color:#fffaf0;"></div>
| + | |
| - | == References ==
| + | |
| - | <references/>
| + | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Polyangium compositum thaxter 1904]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Jin, X]] | + | [[Category: Sorangium cellulosum]] |
| - | [[Category: Khosla, C]] | + | [[Category: Jin X]] |
| - | [[Category: Mathews, I I]] | + | [[Category: Khosla C]] |
| - | [[Category: Wong, F T]] | + | [[Category: Mathews II]] |
| - | [[Category: Acyl carrier protein malonyl coa]] | + | [[Category: Wong FT]] |
| - | [[Category: Acylation]]
| + | |
| - | [[Category: Acyltransferase]]
| + | |
| - | [[Category: Transferase]]
| + | |
