View source for 5cup


==Structure of Rhodopseudomonas palustris PduL - phosphate bound form==
<StructureSection load='5cup' size='340' side='right'caption='[[5cup]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5cup]] 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=5CUP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CUP FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=5cup FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cup OCA], [https://pdbe.org/5cup PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cup RCSB], [https://www.ebi.ac.uk/pdbsum/5cup PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cup ProSAT]</span></td></tr>
</table>
== 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> 
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Rhodopseudomonas palustris BisB18]]
[[Category: Erbilgin O]]
[[Category: Kerfeld CA]]
[[Category: Sutter M]]