8ik2: Difference between revisions

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'''Unreleased structure'''


The entry 8ik2 is ON HOLD  until Paper Publication
==RhlA exhibits dual thioesterase and acyltransferase activities during rhamnolipid biosynthesis==
 
<StructureSection load='8ik2' size='340' side='right'caption='[[8ik2]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
Authors: Tang, T., Fu, L.H., Xie, W.H., Luo, Y.Z., Zhang, Y.T., Si, T.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[8ik2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8IK2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8IK2 FirstGlance]. <br>
Description: RhlA exhibits dual thioesterase and acyltransferase activities during rhamnolipid biosynthesis
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.151&#8491;</td></tr>
[[Category: Unreleased Structures]]
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5UF:(3~{S})-3-OXIDANYLDECANOIC+ACID'>5UF</scene></td></tr>
[[Category: Xie, W.H]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8ik2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ik2 OCA], [https://pdbe.org/8ik2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ik2 RCSB], [https://www.ebi.ac.uk/pdbsum/8ik2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ik2 ProSAT]</span></td></tr>
[[Category: Si, T]]
</table>
[[Category: Zhang, Y.T]]
== Function ==
[[Category: Tang, T]]
[https://www.uniprot.org/uniprot/RHLA_PSEAE RHLA_PSEAE] Required for rhamnolipid surfactant production (PubMed:15126453). Supplies the acyl moieties for rhamnolipid biosynthesis by competing with the enzymes of the type II fatty acid synthase (FASII) cycle for the beta-hydroxyacyl-acyl carrier protein (ACP) pathway intermediates. Catalyzes the formation of one molecule of beta-hydroxydecanoyl-beta-hydroxydecanoate from two molecules of beta-hydroxydecanoyl-ACP. Is the only enzyme required to generate the lipid component of rhamnolipid. In vitro results establish that RhlA is highly selective for 10-carbon acyl-ACP intermediates and thus functions as the molecular ruler that controls the acyl chain composition of rhamnolipids. Cannot use beta-hydroxydecanoyl-CoA as substrate (PubMed:18326581). Rhamnolipid production plays an important role in swarming motility (PubMed:15126453).<ref>PMID:15126453</ref> <ref>PMID:18326581</ref>
[[Category: Fu, L.H]]
== References ==
[[Category: Luo, Y.Z]]
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas aeruginosa PAO1]]
[[Category: Fu LH]]
[[Category: Luo YZ]]
[[Category: Si T]]
[[Category: Tang T]]
[[Category: Xie WH]]
[[Category: Zhang YT]]

Latest revision as of 13:09, 1 November 2023

RhlA exhibits dual thioesterase and acyltransferase activities during rhamnolipid biosynthesis

8ik2, resolution 2.15Å

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