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1eb3

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[[Image:1eb3.gif|left|200px]]<br />
 
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<applet load="1eb3" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1eb3, resolution 1.75&Aring;" />
 
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'''YEAST 5-AMINOLAEVULINIC ACID DEHYDRATASE 4,7-DIOXOSEBACIC ACID COMPLEX'''<br />
 
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==Overview==
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==YEAST 5-AMINOLAEVULINIC ACID DEHYDRATASE 4,7-DIOXOSEBACIC ACID COMPLEX==
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The structures of 5-aminolaevulinic acid dehydratase complexed with two, irreversible inhibitors (4-oxosebacic acid and 4,7-dioxosebacic acid) have, been solved at high resolution. Both inhibitors bind by forming a Schiff, base link with Lys 263 at the active site. Previous inhibitor binding, studies have defined the interactions made by only one of the two, substrate moieties (P-side substrate) which bind to the enzyme during, catalysis. The structures reported here provide an improved definition of, the interactions made by both of the substrate molecules (A- and P-side, substrates). The most intriguing result is the novel finding that, 4,7-dioxosebacic acid forms a second Schiff base with the enzyme involving, Lys 210. It has been known for many years that P-side substrate forms a, Schiff base (with Lys 263) but until now there has been no evidence that, binding of A-side substrate involves formation of a Schiff base with the, enzyme. A catalytic mechanism involving substrate linked to the enzyme, through Schiff bases at both the A- and P-sites is proposed.
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<StructureSection load='1eb3' size='340' side='right'caption='[[1eb3]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1eb3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EB3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EB3 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]] 1.75&#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=DSB:4,7-DIOXOSEBACIC+ACID'>DSB</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1eb3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eb3 OCA], [https://pdbe.org/1eb3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eb3 RCSB], [https://www.ebi.ac.uk/pdbsum/1eb3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eb3 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HEM2_YEAST HEM2_YEAST] Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen.
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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/eb/1eb3_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=1eb3 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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The structures of 5-aminolaevulinic acid dehydratase complexed with two irreversible inhibitors (4-oxosebacic acid and 4,7-dioxosebacic acid) have been solved at high resolution. Both inhibitors bind by forming a Schiff base link with Lys 263 at the active site. Previous inhibitor binding studies have defined the interactions made by only one of the two substrate moieties (P-side substrate) which bind to the enzyme during catalysis. The structures reported here provide an improved definition of the interactions made by both of the substrate molecules (A- and P-side substrates). The most intriguing result is the novel finding that 4,7-dioxosebacic acid forms a second Schiff base with the enzyme involving Lys 210. It has been known for many years that P-side substrate forms a Schiff base (with Lys 263) but until now there has been no evidence that binding of A-side substrate involves formation of a Schiff base with the enzyme. A catalytic mechanism involving substrate linked to the enzyme through Schiff bases at both the A- and P-sites is proposed.
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==About this Structure==
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The X-ray structure of yeast 5-aminolaevulinic acid dehydratase complexed with two diacid inhibitors.,Erskine PT, Coates L, Newbold R, Brindley AA, Stauffer F, Wood SP, Warren MJ, Cooper JB, Shoolingin-Jordan PM, Neier R FEBS Lett. 2001 Aug 17;503(2-3):196-200. PMID:11513881<ref>PMID:11513881</ref>
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1EB3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with ZN and DSB as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Porphobilinogen_synthase Porphobilinogen synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.24 4.2.1.24] Structure known Active Sites: AC1 and AC2. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EB3 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The X-ray structure of yeast 5-aminolaevulinic acid dehydratase complexed with two diacid inhibitors., Erskine PT, Coates L, Newbold R, Brindley AA, Stauffer F, Wood SP, Warren MJ, Cooper JB, Shoolingin-Jordan PM, Neier R, FEBS Lett. 2001 Aug 17;503(2-3):196-200. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11513881 11513881]
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</div>
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[[Category: Porphobilinogen synthase]]
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<div class="pdbe-citations 1eb3" style="background-color:#fffaf0;"></div>
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[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Brindley, A.A.]]
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[[Category: Coates, L.]]
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[[Category: Cooper, J.B.]]
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[[Category: Erskine, P.T.]]
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[[Category: Neier, R.]]
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[[Category: Newbold, R.]]
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[[Category: Shoolingin-Jordan, P.M.]]
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[[Category: Stauffer, F.]]
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[[Category: Warren, M.J.]]
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[[Category: Wood, S.P.]]
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[[Category: DSB]]
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[[Category: ZN]]
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[[Category: aldolase]]
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[[Category: dehydratase]]
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[[Category: tetrapyrrole synthesis]]
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[[Category: tim barrel]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 16:09:56 2007''
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==See Also==
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*[[Porphobilinogen synthase|Porphobilinogen synthase]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Saccharomyces cerevisiae]]
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[[Category: Brindley AA]]
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[[Category: Coates L]]
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[[Category: Cooper JB]]
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[[Category: Erskine PT]]
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[[Category: Neier R]]
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[[Category: Newbold R]]
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[[Category: Shoolingin-Jordan PM]]
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[[Category: Stauffer F]]
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[[Category: Warren MJ]]
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[[Category: Wood SP]]

Current revision

YEAST 5-AMINOLAEVULINIC ACID DEHYDRATASE 4,7-DIOXOSEBACIC ACID COMPLEX

PDB ID 1eb3

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