1ssm

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(New page: 200px<br /><applet load="1ssm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ssm, resolution 2.15&Aring;" /> '''Serine Acetyltransfe...)
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[[Image:1ssm.gif|left|200px]]<br /><applet load="1ssm" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ssm, resolution 2.15&Aring;" />
 
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'''Serine Acetyltransferase- Apoenzyme (truncated)'''<br />
 
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==Overview==
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==Serine Acetyltransferase- Apoenzyme (truncated)==
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Serine 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.
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<StructureSection load='1ssm' size='340' side='right'caption='[[1ssm]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ssm]] is a 6 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=1SSM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SSM FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ssm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ssm OCA], [https://pdbe.org/1ssm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ssm RCSB], [https://www.ebi.ac.uk/pdbsum/1ssm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ssm ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CYSE_HAEIN CYSE_HAEIN]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ss/1ssm_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ssm ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1SSM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Active as [http://en.wikipedia.org/wiki/Serine_O-acetyltransferase Serine O-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.30 2.3.1.30] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SSM OCA].
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*[[Serine acetyltransferase|Serine acetyltransferase]]
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__TOC__
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==Reference==
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</StructureSection>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15147185 15147185]
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[[Category: Haemophilus influenzae]]
[[Category: Haemophilus influenzae]]
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[[Category: Serine O-acetyltransferase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Huang B]]
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[[Category: Huang, B.]]
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[[Category: Olsen LR]]
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[[Category: Olsen, L.R.]]
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[[Category: Roderick SL]]
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[[Category: Roderick, S.L.]]
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[[Category: Vetting MW]]
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[[Category: Vetting, M.W.]]
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[[Category: left-handed parallel beta helix]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:37:53 2007''
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Current revision

Serine Acetyltransferase- Apoenzyme (truncated)

PDB ID 1ssm

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