5cuo: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5cuo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodopseudomonas_palustris_BisB18 Rhodopseudomonas palustris BisB18]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CUO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CUO FirstGlance]. <br>
<table><tr><td colspan='2'>[[5cuo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodopseudomonas_palustris_BisB18 Rhodopseudomonas palustris BisB18]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CUO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CUO FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.544&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=5cuo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cuo OCA], [https://pdbe.org/5cuo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cuo RCSB], [https://www.ebi.ac.uk/pdbsum/5cuo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cuo 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=5cuo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cuo OCA], [https://pdbe.org/5cuo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cuo RCSB], [https://www.ebi.ac.uk/pdbsum/5cuo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cuo ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/PDUL_RHOPB PDUL_RHOPB] Involved in 1,2-propanediol (1,2-PD) utilization within the bacterial microcompartment (BMC) dedicated to 1,2-PD degradation by catalyzing the conversion of propanoyl-CoA to propanoyl-phosphate. CoA is regenerated within the pdu BMC (for use by PduP) via this enzyme, although there must also be cofactor transport across the BMC (PubMed:26959993). Directly targeted to the BMC (By similarity). Phosphate is probably the first substrate to bind in the forward direction. CoA is probably the first substrate to bind in the reverse direction, and might bind to the enzyme as the BMC assembles, ensuring cofactor encapsulation (Probable).[UniProtKB:Q9XDN5]<ref>PMID:26959993</ref> <ref>PMID:26959993</ref>  
[https://www.uniprot.org/uniprot/PDUL_RHOPB PDUL_RHOPB] Involved in 1,2-propanediol (1,2-PD) utilization within the bacterial microcompartment (BMC) dedicated to 1,2-PD degradation by catalyzing the conversion of propanoyl-CoA to propanoyl-phosphate. CoA is regenerated within the pdu BMC (for use by PduP) via this enzyme, although there must also be cofactor transport across the BMC (PubMed:26959993). Directly targeted to the BMC (By similarity). Phosphate is probably the first substrate to bind in the forward direction. CoA is probably the first substrate to bind in the reverse direction, and might bind to the enzyme as the BMC assembles, ensuring cofactor encapsulation (Probable).[UniProtKB:Q9XDN5]<ref>PMID:26959993</ref> <ref>PMID:26959993</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacterial Microcompartments (BMCs) are proteinaceous organelles that encapsulate critical segments of autotrophic and heterotrophic metabolic pathways; they are functionally diverse and are found across 23 different phyla. The majority of catabolic BMCs (metabolosomes) compartmentalize a common core of enzymes to metabolize compounds via a toxic and/or volatile aldehyde intermediate. The core enzyme phosphotransacylase (PTAC) recycles Coenzyme A and generates an acyl phosphate that can serve as an energy source. The PTAC predominantly associated with metabolosomes (PduL) has no sequence homology to the PTAC ubiquitous among fermentative bacteria (Pta). Here, we report two high-resolution PduL crystal structures with bound substrates. The PduL fold is unrelated to that of Pta; it contains a dimetal active site involved in a catalytic mechanism distinct from that of the housekeeping PTAC. Accordingly, PduL and Pta exemplify functional, but not structural, convergent evolution. The PduL structure, in the context of the catalytic core, completes our understanding of the structural basis of cofactor recycling in the metabolosome lumen.
The Structural Basis of Coenzyme A Recycling in a Bacterial Organelle.,Erbilgin O, Sutter M, Kerfeld CA PLoS Biol. 2016 Mar 9;14(3):e1002399. doi: 10.1371/journal.pbio.1002399., eCollection 2016 Mar. PMID:26959993<ref>PMID:26959993</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5cuo" style="background-color:#fffaf0;"></div>
== References ==
== References ==
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