1s80
From Proteopedia
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| - | [[Image:1s80.gif|left|200px]]<br /><applet load="1s80" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1s80, resolution 2.70Å" /> | ||
| - | '''Structure of Serine Acetyltranferase from Haemophilis influenzae Rd'''<br /> | ||
| - | == | + | ==Structure of Serine Acetyltransferase from Haemophilis influenzae Rd== |
| + | <StructureSection load='1s80' size='340' side='right'caption='[[1s80]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1s80]] 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=1S80 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S80 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]] 2.7Å</td></tr> | ||
| + | <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> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1s80 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s80 OCA], [https://pdbe.org/1s80 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s80 RCSB], [https://www.ebi.ac.uk/pdbsum/1s80 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s80 ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/1s80 TOPSAN]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CYSE_HAEIN CYSE_HAEIN] | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/s8/1s80_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=1s80 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
The crystal structure of serine acetyltransferase (SAT) from Haemophilus influenzae Rd determined at 2.7 A resolution is presented. SAT is a member of a family of hexapeptide-containing transferases that contain six-residue tandem repeats (LIV)-G-X(4) that have been shown to form left-handed parallel beta-helices. In the current structure, each protomer is comprised of two domains: an N-terminal alpha-helical domain and a C-terminal left-handed parallel beta-helix domain. Although other members of this protein family are known to form trimeric structures, SAT forms a dimer of trimers in which the trimer interface is mediated through interactions between both the beta-helix domains and N-terminal domains; these trimers dimerize through contacts in the N-terminal domain. All dimer-of-trimer interactions are mediated through amino acids within an N-terminal extension common only to a subset of SATs, suggesting that members of this subfamily may also adopt hexameric structures. Putative active sites are formed by crevices between adjacent protomers in a trimer. Thus, six independent active sites exist in the hexameric enzyme complex. | The crystal structure of serine acetyltransferase (SAT) from Haemophilus influenzae Rd determined at 2.7 A resolution is presented. SAT is a member of a family of hexapeptide-containing transferases that contain six-residue tandem repeats (LIV)-G-X(4) that have been shown to form left-handed parallel beta-helices. In the current structure, each protomer is comprised of two domains: an N-terminal alpha-helical domain and a C-terminal left-handed parallel beta-helix domain. Although other members of this protein family are known to form trimeric structures, SAT forms a dimer of trimers in which the trimer interface is mediated through interactions between both the beta-helix domains and N-terminal domains; these trimers dimerize through contacts in the N-terminal domain. All dimer-of-trimer interactions are mediated through amino acids within an N-terminal extension common only to a subset of SATs, suggesting that members of this subfamily may also adopt hexameric structures. Putative active sites are formed by crevices between adjacent protomers in a trimer. Thus, six independent active sites exist in the hexameric enzyme complex. | ||
| - | + | Structure of serine acetyltransferase from Haemophilus influenzae Rd.,Gorman J, Shapiro L Acta Crystallogr D Biol Crystallogr. 2004 Sep;60(Pt 9):1600-5. Epub 2004, Aug 26. PMID:15333931<ref>PMID:15333931</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1s80" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Serine acetyltransferase|Serine acetyltransferase]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Haemophilus influenzae]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Burley SK]] | ||
| + | [[Category: Gogos A]] | ||
| + | [[Category: Gorman J]] | ||
| + | [[Category: Shapiro L]] | ||
Current revision
Structure of Serine Acetyltransferase from Haemophilis influenzae Rd
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