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| | <StructureSection load='1gjp' size='340' side='right'caption='[[1gjp]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='1gjp' size='340' side='right'caption='[[1gjp]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1gjp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GJP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GJP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1gjp]] 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=1GJP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GJP FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4OX:4-OXODECANEDIOIC+ACID'>4OX</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1aw5|1aw5]], [[1eb3|1eb3]], [[1h7n|1h7n]], [[1h7o|1h7o]], [[1h7p|1h7p]], [[1h7r|1h7r]], [[1qml|1qml]], [[1qnv|1qnv]], [[1ylv|1ylv]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4OX:4-OXODECANEDIOIC+ACID'>4OX</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></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=1gjp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gjp OCA], [https://pdbe.org/1gjp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gjp RCSB], [https://www.ebi.ac.uk/pdbsum/1gjp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gjp ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gjp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gjp OCA], [http://pdbe.org/1gjp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gjp RCSB], [http://www.ebi.ac.uk/pdbsum/1gjp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1gjp ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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. | + | [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. |
| | == 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: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Porphobilinogen synthase]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Brindley, A A]] | + | [[Category: Brindley AA]] |
| - | [[Category: Coates, L]] | + | [[Category: Coates L]] |
| - | [[Category: Cooper, J B]] | + | [[Category: Cooper JB]] |
| - | [[Category: Erskine, P T]] | + | [[Category: Erskine PT]] |
| - | [[Category: Neier, R]] | + | [[Category: Neier R]] |
| - | [[Category: Newbold, R]] | + | [[Category: Newbold R]] |
| - | [[Category: Shoolingin-Jordan, P M]] | + | [[Category: Shoolingin-Jordan PM]] |
| - | [[Category: Warren, M J]] | + | [[Category: Warren MJ]] |
| - | [[Category: Wood, S P]] | + | [[Category: Wood SP]] |
| - | [[Category: Aldolase]]
| + | |
| - | [[Category: Dehydratase]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Tetrapyrrole synthesis]]
| + | |
| - | [[Category: Tim barrel]]
| + | |
| Structural highlights
Function
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.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Erskine PT, Coates L, Newbold R, Brindley AA, Stauffer F, Wood SP, Warren MJ, Cooper JB, Shoolingin-Jordan PM, Neier R. The X-ray structure of yeast 5-aminolaevulinic acid dehydratase complexed with two diacid inhibitors. FEBS Lett. 2001 Aug 17;503(2-3):196-200. PMID:11513881
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