This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


7uwr

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:23, 8 September 2022) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='7uwr' size='340' side='right'caption='[[7uwr]], [[Resolution|resolution]] 2.61&Aring;' scene=''>
<StructureSection load='7uwr' size='340' side='right'caption='[[7uwr]], [[Resolution|resolution]] 2.61&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[7uwr]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7UWR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UWR FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[7uwr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_venezuelae Streptomyces venezuelae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7UWR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UWR FirstGlance]. <br>
</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=7uwr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7uwr OCA], [https://pdbe.org/7uwr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7uwr RCSB], [https://www.ebi.ac.uk/pdbsum/7uwr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7uwr ProSAT]</span></td></tr>
</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=7uwr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7uwr OCA], [https://pdbe.org/7uwr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7uwr RCSB], [https://www.ebi.ac.uk/pdbsum/7uwr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7uwr ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[https://www.uniprot.org/uniprot/PIKA1_STRVZ PIKA1_STRVZ]] Involved in the biosynthesis of 12- and 14-membered ring macrolactone antibiotics such as methymycin and neomethymycin, and pikromycin and narbomycin, respectively. Component of the pikromycin PKS which catalyzes the biosynthesis of both precursors 10-deoxymethynolide (12-membered ring macrolactone) and narbonolide (14-membered ring macrolactone) (PubMed:18512859, PubMed:19437523). Chain elongation through PikAI, PikAII and PikAIII followed by thioesterase catalyzed termination results in the production of 10-deoxymethynolide, while continued elongation through PikAIV, followed by thioesterase (TE) catalyzed cyclization results in the biosynthesis of the narbonolide.<ref>PMID:10421766</ref> <ref>PMID:18512859</ref> <ref>PMID:19437523</ref> <ref>PMID:19027305</ref>
+
[[https://www.uniprot.org/uniprot/PIKA1_STRVZ PIKA1_STRVZ]] Involved in the biosynthesis of 12- and 14-membered ring macrolactone antibiotics such as methymycin and neomethymycin, and pikromycin and narbomycin, respectively. Component of the pikromycin PKS which catalyzes the biosynthesis of both precursors 10-deoxymethynolide (12-membered ring macrolactone) and narbonolide (14-membered ring macrolactone) (PubMed:18512859, PubMed:19437523). Chain elongation through PikAI, PikAII and PikAIII followed by thioesterase catalyzed termination results in the production of 10-deoxymethynolide, while continued elongation through PikAIV, followed by thioesterase (TE) catalyzed cyclization results in the biosynthesis of the narbonolide.<ref>PMID:10421766</ref> <ref>PMID:18512859</ref> <ref>PMID:19437523</ref> <ref>PMID:19027305</ref>
-
<div style="background-color:#fffaf0;">
+
-
== Publication Abstract from PubMed ==
+
-
The first domain of modular polyketide synthases (PKSs) is most commonly a ketosynthase (KS)-like enzyme, KS(Q), that primes polyketide synthesis. Unlike downstream KSs that fuse alpha-carboxyacyl groups to growing polyketide chains, it performs an extension-decoupled decarboxylation of these groups to generate primer units. When Pik127, a model triketide synthase constructed from modules of the pikromycin synthase, was studied by cryoelectron microscopy (cryo-EM), the dimeric didomain comprised of KS(Q) and the neighboring methylmalonyl-selective acyltransferase (AT) dominated the class averages and yielded structures at 2.5- and 2.8-A resolution, respectively. Comparisons with ketosynthases complexed with their substrates revealed the conformation of the (2S)-methylmalonyl-S-phosphopantetheinyl portion of KS(Q) and KS substrates prior to decarboxylation. Point mutants of Pik127 probed the roles of residues in the KS(Q) active site, while an AT-swapped version of Pik127 demonstrated that KS(Q) can also decarboxylate malonyl groups. Mechanisms for how KS(Q) and KS domains catalyze carbon-carbon chemistry are proposed.
+
-
 
+
-
Priming enzymes from the pikromycin synthase reveal how assembly-line ketosynthases catalyze carbon-carbon chemistry.,Dickinson MS, Miyazawa T, McCool RS, Keatinge-Clay AT Structure. 2022 Jun 13. pii: S0969-2126(22)00230-1. doi:, 10.1016/j.str.2022.05.021. PMID:35738283<ref>PMID:35738283</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 7uwr" style="background-color:#fffaf0;"></div>
+
== References ==
== References ==
<references/>
<references/>
Line 22: Line 13:
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Dickinson, M S]]
+
[[Category: Streptomyces venezuelae]]
-
[[Category: Keatinge-Clay, A T]]
+
[[Category: Dickinson MS]]
-
[[Category: McCool, R S]]
+
[[Category: Keatinge-Clay AT]]
-
[[Category: Miyazawa, T]]
+
[[Category: McCool RS]]
-
[[Category: Acyltransferase]]
+
[[Category: Miyazawa T]]
-
[[Category: Biosynthetic protein]]
+
-
[[Category: Decarboxylation]]
+
-
[[Category: Ketosynthase-like]]
+

Current revision

KSQ+AT from first module of the pikromycin synthase

PDB ID 7uwr

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/7uwr"
Personal tools