View source for 4ybo


==Structure of Citrate Synthase from the Thermoacidophilic Euryarchaeon Thermolasma acidophilum==
<StructureSection load='4ybo' size='340' side='right'caption='[[4ybo]], [[Resolution|resolution]] 2.18&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ybo]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoplasma_acidophilum_DSM_1728 Thermoplasma acidophilum DSM 1728]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YBO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YBO 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]] 2.179&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCT:BICARBONATE+ION'>BCT</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=4ybo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ybo OCA], [https://pdbe.org/4ybo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ybo RCSB], [https://www.ebi.ac.uk/pdbsum/4ybo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ybo ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CISY_THEAC CISY_THEAC] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Citrate synthase (CS) plays a central metabolic role in aerobes and many other organisms. The CS reaction comprises two half-reactions: a Claisen aldol condensation of acetyl-CoA (AcCoA) and oxaloacetate (OAA) that forms citryl-CoA (CitCoA), and CitCoA hydrolysis. Protein conformational changes that `close' the active site play an important role in the assembly of a catalytically competent condensation active site. CS from the thermoacidophile Thermoplasma acidophilum (TpCS) possesses an endogenous Trp fluorophore that can be used to monitor the condensation reaction. The 2.2 A resolution crystal structure of TpCS fused to a C-terminal hexahistidine tag (TpCSH6) reported here is an `open' structure that, when compared with several liganded TpCS structures, helps to define a complete path for active-site closure. One active site in each dimer binds a neighboring His tag, the first nonsubstrate ligand known to occupy both the AcCoA and OAA binding sites. Solution data collectively suggest that this fortuitous interaction is stabilized by the crystalline lattice. As a polar but almost neutral ligand, the active site-tail interaction provides a new starting point for the design of bisubstrate-analog inhibitors of CS.

An active site-tail interaction in the structure of hexahistidine-tagged Thermoplasma acidophilum citrate synthase.,Murphy JR, Donini S, Kappock TJ Acta Crystallogr F Struct Biol Commun. 2015 Oct;71(Pt 10):1292-9. doi:, 10.1107/S2053230X15015939. Epub 2015 Sep 23. PMID:26457521<ref>PMID:26457521</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ybo" style="background-color:#fffaf0;"></div>

==See Also==
*[[Citrate Synthase 3D structures|Citrate Synthase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermoplasma acidophilum DSM 1728]]
[[Category: Donini S]]
[[Category: Kappock TJ]]
[[Category: Murphy JR]]