1sst: Difference between revisions
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<StructureSection load='1sst' size='340' side='right'caption='[[1sst]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1sst' size='340' side='right'caption='[[1sst]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1sst]] is a 3 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1sst]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SST OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SST FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene></td></tr> | |||
<tr id=' | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1sst FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sst OCA], [https://pdbe.org/1sst PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sst RCSB], [https://www.ebi.ac.uk/pdbsum/1sst PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sst ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/CYSE_HAEIN CYSE_HAEIN] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Haemophilus influenzae]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Huang B]] | |||
[[Category: Huang | [[Category: Olsen LR]] | ||
[[Category: Olsen | [[Category: Roderick SL]] | ||
[[Category: Roderick | [[Category: Vetting MW]] | ||
[[Category: Vetting | |||
Latest revision as of 09:20, 23 August 2023
Serine Acetyltransferase- Complex with CoASerine Acetyltransferase- Complex with CoA
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedSerine acetyltransferase (SAT, EC 2.3.1.30) catalyzes the CoA-dependent acetylation of the side chain hydroxyl group of l-serine to form O-acetylserine, as the first step of a two-step biosynthetic pathway in bacteria and plants leading to the formation of l-cysteine. This reaction represents a key metabolic point of regulation for the cysteine biosynthetic pathway due to its feedback inhibition by cysteine. We have determined the X-ray crystal structure of Haemophilus influenzae SAT in complexes with CoA and its cysteine feedback inhibitor. The enzyme is a 175 kDa hexamer displaying the characteristic left-handed parallel beta-helix (LbetaH) structural domain of the hexapeptide acyltransferase superfamily of enzymes. Cysteine is bound in a crevice between adjacent LbetaH domains and underneath a loop excluded from the coiled LbetaH. The proximity of its thiol group to the thiol group of CoA derived from superimposed models of the cysteine and CoA complexes confirms that cysteine is bound at the active site. Analysis of the contacts of SAT with cysteine and CoA and the conformational differences that distinguish these complexes provides a structural basis for cysteine feedback inhibition, which invokes competition between cysteine and serine binding and a cysteine-induced conformational change of the C-terminal segment of the enzyme that excludes binding of the cofactor. Structure of serine acetyltransferase in complexes with CoA and its cysteine feedback inhibitor.,Olsen LR, Huang B, Vetting MW, Roderick SL Biochemistry. 2004 May 25;43(20):6013-9. PMID:15147185[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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