View source for 5jis


==The Crystal Structure of O-acetyl serine sulfhydralase from Brucella abortus==
<StructureSection load='5jis' size='340' side='right'caption='[[5jis]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5jis]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Brucella_abortus_S19 Brucella abortus S19]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JIS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JIS 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</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=5jis FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jis OCA], [https://pdbe.org/5jis PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jis RCSB], [https://www.ebi.ac.uk/pdbsum/5jis PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jis ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0F6AQU1_BRUA1 A0A0F6AQU1_BRUA1] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cysteine biosynthesis takes place via a two-step pathway in bacteria, fungi, plants and protozoan parasites, but not in humans, and hence, the machinery of cysteine biosynthesis is an opportune target for therapeutics. The decameric cysteine synthase complex (CSC) is formed when the C-terminal tail of serine acetyltransferase (SAT) binds in the active site of O-acetylserine sulfydrylase (OASS), playing a role in the regulation of this pathway. Here, we show that OASS from Brucella abortus (BaOASS) does not interact with its cognate SAT C-terminal tail. Crystal structures of native BaOASS showed that residues Gln96 and Tyr125 occupy the active-site pocket and interfere with the entry of the SAT C-terminal tail. The BaOASS (Q96A-Y125A) mutant showed relatively strong binding (Kd = 32.4 muM) to BaSAT C-terminal peptides in comparison with native BaOASS. The mutant structure looks similar except that the active-site pocket has enough space to bind the SAT C-terminal end. Surface plasmon resonance results showed a relatively strong (7.3 muM Kd) interaction between BaSAT and the BaOASS (Q96A-Y125A), but no interaction with native BaOASS. Taken together, our observations suggest that the CSC does not form in B. abortus.

Structure-based mutational studies of O-acetylserine sulfhydrylase reveal the reason for the loss of cysteine synthase complex formation in Brucella abortus.,Dharavath S, Raj I, Gourinath S Biochem J. 2017 Mar 23;474(7):1221-1239. doi: 10.1042/BCJ20161062. PMID:28126739<ref>PMID:28126739</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5jis" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Brucella abortus S19]]
[[Category: Large Structures]]
[[Category: Dharavath S]]
[[Category: Gourinath S]]