View source for 7ra4


==Crystal structure of Neisseria gonorrhoeae serine acetyltransferase (CysE) in complex with serine==
<StructureSection load='7ra4' size='340' side='right'caption='[[7ra4]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7ra4]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_gonorrhoeae_FA_1090 Neisseria gonorrhoeae FA 1090]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7RA4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RA4 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]] 2.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SER:SERINE'>SER</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=7ra4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ra4 OCA], [https://pdbe.org/7ra4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ra4 RCSB], [https://www.ebi.ac.uk/pdbsum/7ra4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ra4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q5F6X0_NEIG1 Q5F6X0_NEIG1] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Serine acetyltransferase (SAT) catalyzes the first step in the two-step pathway to synthesize L-cysteine in bacteria and plants. SAT synthesizes O-acetylserine from substrates Lserine and acetyl coenzyme A and is a key enzyme for regulating cellular cysteine levels by feedback inhibition of L-cysteine, and its involvement in the cysteine synthase complex. We have performed extensive structural and kinetic characterization of the SAT enzyme from the antibiotic-resistant pathogen Neisseria gonorrhoeae. Using X-ray crystallography, we have solved the structures of NgSAT with the non-natural ligand, L-malate (present in the crystallization screen) to 2.01 A and with the natural substrate L-serine (2.80 A) bound. Both structures are hexamers, with each monomer displaying the characteristic left-handed parallel beta-helix domain of the acyltransferase superfamily of enzymes. Each structure displays both extended and closed conformations of the C-terminal tail. &#160;Lmalate bound in the active site results in an interesting mix of open and closed active site conformations, exhibiting a structural change mimicking the conformation of cysteine (inhibitor) bound structures from other organisms. Kinetic characterization shows competitive inhibition of L-cysteine with substrates L-serine and acetyl coenzyme A. The SAT reaction represents a key point for the regulation of cysteine biosynthesis and controlling cellular sulfur due to feedback inhibition by L-cysteine and formation of the cysteine synthase complex. Data presented here provide the structural and mechanistic basis for inhibitor design and given this enzyme is not present in humans could be explored to combat the rise of extensively antimicrobial-resistant N. gonorrhoeae.

Serine acetyltransferase from Neisseria gonorrhoeae; structural and biochemical basis of inhibition.,Oldham KEA, Prentice EJ, Summers EL, Hicks JL Biochem J. 2021 Dec 10. pii: 230431. doi: 10.1042/BCJ20210564. PMID:34890451<ref>PMID:34890451</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7ra4" style="background-color:#fffaf0;"></div>

==See Also==
*[[Serine acetyltransferase|Serine acetyltransferase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Neisseria gonorrhoeae FA 1090]]
[[Category: Hicks JL]]
[[Category: Oldham KE]]
[[Category: Prentice EJ]]
[[Category: Summers EL]]