4hzc: Difference between revisions
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The | ==Crystal structure of Serine acetyltransferase from Brucella abortus strain S19== | ||
<StructureSection load='4hzc' size='340' side='right'caption='[[4hzc]], [[Resolution|resolution]] 1.97Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4hzc]] is a 12 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=4HZC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HZC 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]] 1.97Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=15P:POLYETHYLENE+GLYCOL+(N=34)'>15P</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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=4hzc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hzc OCA], [https://pdbe.org/4hzc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hzc RCSB], [https://www.ebi.ac.uk/pdbsum/4hzc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hzc ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A0F6AR69_BRUA1 A0A0F6AR69_BRUA1] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Brucella abortus is the major cause of premature foetal abortion in cattle, can be transmitted from cattle to humans, and is considered a powerful biological weapon. De novo cysteine biosynthesis is one of the essential pathways reported in bacteria, protozoa, and plants. Serine acetyltransferase (SAT) initiates this reaction by catalyzing the formation of O-acetylserine (OAS) using l-serine and acetyl coenzyme A as substrates. Here we report kinetic and crystallographic studies of this enzyme from B. abortus. The kinetic studies indicate that cysteine competitively inhibits the binding of serine to B. abortus SAT (BaSAT) and noncompetitively inhibits the binding of acetyl coenzyme A. The crystal structures of BaSAT in its apo state and in complex with coenzyme A (CoA) were determined to 1.96A and 1.87A resolution, respectively. BaSAT was observed as a trimer in a size exclusion column; however, it was seen as a hexamer in dynamic light scattering (DLS) studies and in the crystal structure, indicating it may exist in both states. The complex structure shows coenzyme A bound to the C-terminal region, making mostly hydrophobic contacts from the center of the active site extending up to the surface of the protein. There is no conformational difference in the enzyme between the apo and the complexed states, indicating lock and key binding and the absence of an induced fit mechanism. | |||
Crystal structure of serine acetyl transferase from Brucella abortus and its complex with coenzyme A.,Kumar S, Kumar N, Alam N, Gourinath S Biochim Biophys Acta. 2014 Jul 22;1844(10):1741-1748. doi:, 10.1016/j.bbapap.2014.07.009. PMID:25058332<ref>PMID:25058332</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4hzc" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Serine acetyltransferase|Serine acetyltransferase]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Brucella abortus S19]] | |||
[[Category: Large Structures]] | |||
[[Category: Kumar S]] | |||
[[Category: Samudrala G]] | |||
Latest revision as of 13:05, 30 October 2024
Crystal structure of Serine acetyltransferase from Brucella abortus strain S19Crystal structure of Serine acetyltransferase from Brucella abortus strain S19
Structural highlights
FunctionPublication Abstract from PubMedBrucella abortus is the major cause of premature foetal abortion in cattle, can be transmitted from cattle to humans, and is considered a powerful biological weapon. De novo cysteine biosynthesis is one of the essential pathways reported in bacteria, protozoa, and plants. Serine acetyltransferase (SAT) initiates this reaction by catalyzing the formation of O-acetylserine (OAS) using l-serine and acetyl coenzyme A as substrates. Here we report kinetic and crystallographic studies of this enzyme from B. abortus. The kinetic studies indicate that cysteine competitively inhibits the binding of serine to B. abortus SAT (BaSAT) and noncompetitively inhibits the binding of acetyl coenzyme A. The crystal structures of BaSAT in its apo state and in complex with coenzyme A (CoA) were determined to 1.96A and 1.87A resolution, respectively. BaSAT was observed as a trimer in a size exclusion column; however, it was seen as a hexamer in dynamic light scattering (DLS) studies and in the crystal structure, indicating it may exist in both states. The complex structure shows coenzyme A bound to the C-terminal region, making mostly hydrophobic contacts from the center of the active site extending up to the surface of the protein. There is no conformational difference in the enzyme between the apo and the complexed states, indicating lock and key binding and the absence of an induced fit mechanism. Crystal structure of serine acetyl transferase from Brucella abortus and its complex with coenzyme A.,Kumar S, Kumar N, Alam N, Gourinath S Biochim Biophys Acta. 2014 Jul 22;1844(10):1741-1748. doi:, 10.1016/j.bbapap.2014.07.009. PMID:25058332[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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