3our: Difference between revisions

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'''Unreleased structure'''


The entry 3our is ON HOLD  until Paper Publication
==Crystal structure of complex between EIIA and a novel pyruvate decarboxylase==
<StructureSection load='3our' size='340' side='right'caption='[[3our]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3our]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_vulnificus_CMCP6 Vibrio vulnificus CMCP6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OUR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OUR 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]] 2.2&#8491;</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=3our FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3our OCA], [https://pdbe.org/3our PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3our RCSB], [https://www.ebi.ac.uk/pdbsum/3our PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3our ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FRSA_VIBVU FRSA_VIBVU] Catalyzes the hydrolysis of esters (PubMed:30951551). In vitro, prefers short chain alkanoate ester as substrate. Displays highest activity towards p-nitrophenyl acetate (pNPA). Has weaker activity towards p-nitrophenyl butyrate (pNPB) (PubMed:30951551).<ref>PMID:30951551</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The interaction between fermentation-respiration switch (FrsA) protein and glucose-specific enzyme IIA(Glc) increases glucose fermentation under oxygen-limited conditions. We show that FrsA converts pyruvate to acetaldehyde and carbon dioxide in a cofactor-independent manner and that its pyruvate decarboxylation activity is enhanced by the dephosphorylated form of IIA(Glc) (d-IIA(Glc)). Crystal structures of FrsA and its complex with d-IIA(Glc) revealed residues required for catalysis as well as the structural basis for the activation by d-IIA(Glc).


Authors: Jeong, C.-S., An, Y.J., Cha, S.-S.
FrsA functions as a cofactor-independent decarboxylase to control metabolic flux.,Lee KJ, Jeong CS, An YJ, Lee HJ, Park SJ, Seok YJ, Kim P, Lee JH, Lee KH, Cha SS Nat Chem Biol. 2011 May 29. PMID:21623357<ref>PMID:21623357</ref>


Description: Crystal structure of complex between EIIA and a novel pyruvate decarboxylase
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3our" style="background-color:#fffaf0;"></div>


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Oct 20 06:21:14 2010''
==See Also==
*[[Phosphotransferase 3D structures|Phosphotransferase 3D structures]]
*[[Pyruvate decarboxylase|Pyruvate decarboxylase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Vibrio vulnificus CMCP6]]
[[Category: An YJ]]
[[Category: Cha SS]]
[[Category: Jeong CS]]

Latest revision as of 19:57, 1 November 2023

Crystal structure of complex between EIIA and a novel pyruvate decarboxylaseCrystal structure of complex between EIIA and a novel pyruvate decarboxylase

Structural highlights

3our is a 8 chain structure with sequence from Vibrio vulnificus CMCP6. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FRSA_VIBVU Catalyzes the hydrolysis of esters (PubMed:30951551). In vitro, prefers short chain alkanoate ester as substrate. Displays highest activity towards p-nitrophenyl acetate (pNPA). Has weaker activity towards p-nitrophenyl butyrate (pNPB) (PubMed:30951551).[1]

Publication Abstract from PubMed

The interaction between fermentation-respiration switch (FrsA) protein and glucose-specific enzyme IIA(Glc) increases glucose fermentation under oxygen-limited conditions. We show that FrsA converts pyruvate to acetaldehyde and carbon dioxide in a cofactor-independent manner and that its pyruvate decarboxylation activity is enhanced by the dephosphorylated form of IIA(Glc) (d-IIA(Glc)). Crystal structures of FrsA and its complex with d-IIA(Glc) revealed residues required for catalysis as well as the structural basis for the activation by d-IIA(Glc).

FrsA functions as a cofactor-independent decarboxylase to control metabolic flux.,Lee KJ, Jeong CS, An YJ, Lee HJ, Park SJ, Seok YJ, Kim P, Lee JH, Lee KH, Cha SS Nat Chem Biol. 2011 May 29. PMID:21623357[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Wang X, Li ZM, Li Q, Shi M, Bao L, Xu D, Li Z. Purification and biochemical characterization of FrsA protein from Vibrio vulnificus as an esterase. PLoS One. 2019 Apr 5;14(4):e0215084. PMID:30951551 doi:10.1371/journal.pone.0215084
  2. ↑ Lee KJ, Jeong CS, An YJ, Lee HJ, Park SJ, Seok YJ, Kim P, Lee JH, Lee KH, Cha SS. FrsA functions as a cofactor-independent decarboxylase to control metabolic flux. Nat Chem Biol. 2011 May 29. PMID:21623357 doi:10.1038/nchembio.589

3our, resolution 2.20Å

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