1t3d

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[[Image:1t3d.jpg|left|200px]]
 
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{{Structure
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==Crystal structure of Serine Acetyltransferase from E.coli at 2.2A==
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|PDB= 1t3d |SIZE=350|CAPTION= <scene name='initialview01'>1t3d</scene>, resolution 2.20&Aring;
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<StructureSection load='1t3d' size='340' side='right'caption='[[1t3d]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CYS:CYSTEINE'>CYS</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
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<table><tr><td colspan='2'>[[1t3d]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T3D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T3D FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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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]] 2.2&#8491;</td></tr>
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|GENE= CYSE, B3607, C4429, Z5034, ECS4485, SF3646, S4122 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CYS:CYSTEINE'>CYS</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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|DOMAIN=
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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=1t3d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t3d OCA], [https://pdbe.org/1t3d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t3d RCSB], [https://www.ebi.ac.uk/pdbsum/1t3d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t3d ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1t3d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t3d OCA], [http://www.ebi.ac.uk/pdbsum/1t3d PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1t3d RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/CYSE_ECOLI CYSE_ECOLI]
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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/t3/1t3d_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1t3d ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Serine acetyltransferase (SAT) catalyzes the first step of cysteine synthesis in microorganisms and higher plants. Here we present the 2.2 A crystal structure of SAT from Escherichia coli, which is a dimer of trimers, in complex with cysteine. The SAT monomer consists of an amino-terminal alpha-helical domain and a carboxyl-terminal left-handed beta-helix. We identify His(158) and Asp(143) as essential residues that form a catalytic triad with the substrate for acetyl transfer. This structure shows the mechanism by which cysteine inhibits SAT activity and thus controls its own synthesis. Cysteine is found to bind at the serine substrate site and not the acetyl-CoA site that had been reported previously. On the basis of the geometry around the cysteine binding site, we are able to suggest a mechanism for the O-acetylation of serine by SAT. We also compare the structure of SAT with other left-handed beta-helical structures.
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'''Crystal structure of Serine Acetyltransferase from E.coli at 2.2A'''
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The structure and mechanism of serine acetyltransferase from Escherichia coli.,Pye VE, Tingey AP, Robson RL, Moody PC J Biol Chem. 2004 Sep 24;279(39):40729-36. Epub 2004 Jul 1. PMID:15231846<ref>PMID:15231846</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1t3d" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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Serine acetyltransferase (SAT) catalyzes the first step of cysteine synthesis in microorganisms and higher plants. Here we present the 2.2 A crystal structure of SAT from Escherichia coli, which is a dimer of trimers, in complex with cysteine. The SAT monomer consists of an amino-terminal alpha-helical domain and a carboxyl-terminal left-handed beta-helix. We identify His(158) and Asp(143) as essential residues that form a catalytic triad with the substrate for acetyl transfer. This structure shows the mechanism by which cysteine inhibits SAT activity and thus controls its own synthesis. Cysteine is found to bind at the serine substrate site and not the acetyl-CoA site that had been reported previously. On the basis of the geometry around the cysteine binding site, we are able to suggest a mechanism for the O-acetylation of serine by SAT. We also compare the structure of SAT with other left-handed beta-helical structures.
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*[[Serine acetyltransferase|Serine acetyltransferase]]
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== References ==
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==About this Structure==
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<references/>
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1T3D is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T3D OCA].
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__TOC__
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</StructureSection>
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==Reference==
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The structure and mechanism of serine acetyltransferase from Escherichia coli., Pye VE, Tingey AP, Robson RL, Moody PC, J Biol Chem. 2004 Sep 24;279(39):40729-36. Epub 2004 Jul 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15231846 15231846]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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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: Moody PCE]]
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[[Category: Moody, P C.]]
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[[Category: Pye VE]]
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[[Category: Pye, V E.]]
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[[Category: Robson RL]]
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[[Category: Robson, R L.]]
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[[Category: Tingey AP]]
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[[Category: Tingey, A P.]]
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[[Category: dimer of trimer]]
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[[Category: left-handed-beta-helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:50:41 2008''
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Current revision

Crystal structure of Serine Acetyltransferase from E.coli at 2.2A

PDB ID 1t3d

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