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| | <StructureSection load='6iyt' size='340' side='right'caption='[[6iyt]], [[Resolution|resolution]] 1.78Å' scene=''> | | <StructureSection load='6iyt' size='340' side='right'caption='[[6iyt]], [[Resolution|resolution]] 1.78Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6iyt]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_albus_subsp._albus Streptomyces albus subsp. albus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IYT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6IYT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6iyt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_albus_subsp._albus Streptomyces albus subsp. albus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IYT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IYT FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">salAIX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=67257 Streptomyces albus subsp. albus])</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]] 1.78Å</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=6iyt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6iyt OCA], [http://pdbe.org/6iyt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6iyt RCSB], [http://www.ebi.ac.uk/pdbsum/6iyt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6iyt 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=6iyt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6iyt OCA], [https://pdbe.org/6iyt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6iyt RCSB], [https://www.ebi.ac.uk/pdbsum/6iyt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6iyt ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/H1ZZU1_9ACTN H1ZZU1_9ACTN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Streptomyces albus subsp. albus]] | | [[Category: Streptomyces albus subsp. albus]] |
| - | [[Category: Zhang, F]] | + | [[Category: Zhang F]] |
| - | [[Category: Zheng, J]] | + | [[Category: Zheng J]] |
| - | [[Category: Acyltransferase]]
| + | |
| - | [[Category: Ethylhmalonyl-coenzyme some]]
| + | |
| - | [[Category: Polyketide]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
H1ZZU1_9ACTN
Publication Abstract from PubMed
Salinomycin with antibacterial and anticoccidial activities is a commercial polyether polyketide widely used in animal husbandry as a food additive. Malonyl-CoA (MCoA), methylmalonyl-CoA (MMCoA), and ethylmalonyl-CoA (EMCoA) are used as extension units in its biosynthesis. To understand how the salinomycin modular polyketide synthase (PKS) strictly discriminates among these extension units, the acyltransferase (AT) domains selecting MCoA, MMCoA, and EMCoA were structurally characterized. Molecular dynamics simulations of the AT structures helped to reveal the key interactions involved in enzyme-substrate recognitions, which enabled the engineering of AT mutants with switched specificity. The catalytic efficiencies ( kcat/ Km) of these AT mutants are comparable with those of the wild-type AT domains. These results set the stage for engineering the AT substrate specificity of modular PKSs.
Structural Insights into the Substrate Specificity of Acyltransferases from Salinomycin Polyketide Synthase.,Zhang F, Shi T, Ji H, Ali I, Huang S, Deng Z, Min Q, Bai L, Zhao Y, Zheng J Biochemistry. 2019 Jun 19. doi: 10.1021/acs.biochem.9b00305. PMID:31199122[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhang F, Shi T, Ji H, Ali I, Huang S, Deng Z, Min Q, Bai L, Zhao Y, Zheng J. Structural Insights into the Substrate Specificity of Acyltransferases from Salinomycin Polyketide Synthase. Biochemistry. 2019 Jun 19. doi: 10.1021/acs.biochem.9b00305. PMID:31199122 doi:http://dx.doi.org/10.1021/acs.biochem.9b00305
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