4zdn: Difference between revisions
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<StructureSection load='4zdn' size='340' side='right' caption='[[4zdn]], [[Resolution|resolution]] 2.51Å' scene=''> | ==Streptomyces platensis isomigrastatin ketosynthase domain MgsF KS4== | ||
<StructureSection load='4zdn' size='340' side='right'caption='[[4zdn]], [[Resolution|resolution]] 2.51Å' scene=''> | |||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4zdn]] is a 1 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4tl2 4tl2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZDN OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[4zdn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_platensis_subsp._rosaceus Streptomyces platensis subsp. rosaceus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4tl2 4tl2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZDN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZDN FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=4zdn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zdn OCA], [https://pdbe.org/4zdn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zdn RCSB], [https://www.ebi.ac.uk/pdbsum/4zdn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zdn ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/D0U2E4_STRPT D0U2E4_STRPT] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Acyltransferase (AT)-less type I polyketide synthases (PKSs) break the type I PKS paradigm. They lack the integrated AT domains within their modules and instead use a discrete AT that acts in trans, whereas a type I PKS module minimally contains AT, acyl carrier protein (ACP), and ketosynthase (KS) domains. Structures of canonical type I PKS KS-AT didomains reveal structured linkers that connect the two domains. AT-less type I PKS KSs have remnants of these linkers, which have been hypothesized to be AT docking domains. Natural products produced by AT-less type I PKSs are very complex because of an increased representation of unique modifying domains. AT-less type I PKS KSs possess substrate specificity and fall into phylogenetic clades that correlate with their substrates, whereas canonical type I PKS KSs are monophyletic. We have solved crystal structures of seven AT-less type I PKS KS domains that represent various sequence clusters, revealing insight into the large structural and subtle amino acid residue differences that lead to unique active site topologies and substrate specificities. One set of structures represents a larger group of KS domains from both canonical and AT-less type I PKSs that accept amino acid-containing substrates. One structure has a partial AT-domain, revealing the structural consequences of a type I PKS KS evolving into an AT-less type I PKS KS. These structures highlight the structural diversity within the AT-less type I PKS KS family, and most important, provide a unique opportunity to study the molecular evolution of substrate specificity within the type I PKSs. | |||
Structural and evolutionary relationships of "AT-less" type I polyketide synthase ketosynthases.,Lohman JR, Ma M, Osipiuk J, Nocek B, Kim Y, Chang C, Cuff M, Mack J, Bigelow L, Li H, Endres M, Babnigg G, Joachimiak A, Phillips GN Jr, Shen B Proc Natl Acad Sci U S A. 2015 Oct 13;112(41):12693-8. doi:, 10.1073/pnas.1515460112. Epub 2015 Sep 29. PMID:26420866<ref>PMID:26420866</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4zdn" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Streptomyces platensis subsp. rosaceus]] | ||
[[Category: | [[Category: Bingman CA]] | ||
[[Category: | [[Category: Chang C]] | ||
[[Category: | [[Category: Endres M]] | ||
[[Category: | [[Category: Joachimiak A]] | ||
[[Category: | [[Category: Li H]] | ||
[[Category: | [[Category: Lohman JR]] | ||
[[Category: | [[Category: Ma M]] | ||
[[Category: Phillips | [[Category: Phillips Jr GN]] | ||
[[Category: Shen | [[Category: Shen B]] | ||
[[Category: Yennamalli | [[Category: Yennamalli R]] | ||
Latest revision as of 10:30, 22 March 2023
Streptomyces platensis isomigrastatin ketosynthase domain MgsF KS4Streptomyces platensis isomigrastatin ketosynthase domain MgsF KS4
Structural highlights
FunctionPublication Abstract from PubMedAcyltransferase (AT)-less type I polyketide synthases (PKSs) break the type I PKS paradigm. They lack the integrated AT domains within their modules and instead use a discrete AT that acts in trans, whereas a type I PKS module minimally contains AT, acyl carrier protein (ACP), and ketosynthase (KS) domains. Structures of canonical type I PKS KS-AT didomains reveal structured linkers that connect the two domains. AT-less type I PKS KSs have remnants of these linkers, which have been hypothesized to be AT docking domains. Natural products produced by AT-less type I PKSs are very complex because of an increased representation of unique modifying domains. AT-less type I PKS KSs possess substrate specificity and fall into phylogenetic clades that correlate with their substrates, whereas canonical type I PKS KSs are monophyletic. We have solved crystal structures of seven AT-less type I PKS KS domains that represent various sequence clusters, revealing insight into the large structural and subtle amino acid residue differences that lead to unique active site topologies and substrate specificities. One set of structures represents a larger group of KS domains from both canonical and AT-less type I PKSs that accept amino acid-containing substrates. One structure has a partial AT-domain, revealing the structural consequences of a type I PKS KS evolving into an AT-less type I PKS KS. These structures highlight the structural diversity within the AT-less type I PKS KS family, and most important, provide a unique opportunity to study the molecular evolution of substrate specificity within the type I PKSs. Structural and evolutionary relationships of "AT-less" type I polyketide synthase ketosynthases.,Lohman JR, Ma M, Osipiuk J, Nocek B, Kim Y, Chang C, Cuff M, Mack J, Bigelow L, Li H, Endres M, Babnigg G, Joachimiak A, Phillips GN Jr, Shen B Proc Natl Acad Sci U S A. 2015 Oct 13;112(41):12693-8. doi:, 10.1073/pnas.1515460112. Epub 2015 Sep 29. PMID:26420866[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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