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| | <StructureSection load='4v7g' size='340' side='right'caption='[[4v7g]], [[Resolution|resolution]] 3.50Å' scene=''> | | <StructureSection load='4v7g' size='340' side='right'caption='[[4v7g]], [[Resolution|resolution]] 3.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4v7g]] is a 90 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_cereus_var._anthracis"_(cohn_1872)_smith_et_al._1946 "bacillus cereus var. anthracis" (cohn 1872) smith et al. 1946]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vsw 1vsw], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vsx 1vsx] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3jv8 3jv8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V7G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4V7G FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4v7g]] is a 90 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_anthracis Bacillus anthracis]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vsw 1vsw], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vsx 1vsx] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3jv8 3jv8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V7G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V7G FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ribH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1392 "Bacillus cereus var. anthracis" (Cohn 1872) Smith et al. 1946])</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=4v7g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v7g OCA], [https://pdbe.org/4v7g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v7g RCSB], [https://www.ebi.ac.uk/pdbsum/4v7g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v7g ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/6,7-dimethyl-8-ribityllumazine_synthase 6,7-dimethyl-8-ribityllumazine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.78 2.5.1.78] </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=4v7g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v7g OCA], [http://pdbe.org/4v7g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4v7g RCSB], [http://www.ebi.ac.uk/pdbsum/4v7g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4v7g ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RISB_BACAN RISB_BACAN]] Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.[HAMAP-Rule:MF_00178]<ref>PMID:20823551</ref> | + | [https://www.uniprot.org/uniprot/RISB_BACAN RISB_BACAN] Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.[HAMAP-Rule:MF_00178]<ref>PMID:20823551</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: 6,7-dimethyl-8-ribityllumazine synthase]] | + | [[Category: Bacillus anthracis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bacher, A]] | + | [[Category: Bacher A]] |
| - | [[Category: Cushman, M]] | + | [[Category: Cushman M]] |
| - | [[Category: Fischer, M]] | + | [[Category: Fischer M]] |
| - | [[Category: Illarionov, B]] | + | [[Category: Illarionov B]] |
| - | [[Category: Ladenstein, R]] | + | [[Category: Ladenstein R]] |
| - | [[Category: Morgunova, E]] | + | [[Category: Morgunova E]] |
| - | [[Category: Popov, A]] | + | [[Category: Popov A]] |
| - | [[Category: Saller, S]] | + | [[Category: Saller S]] |
| - | [[Category: Sambaiah, T]] | + | [[Category: Sambaiah T]] |
| - | [[Category: Riboflavin biosynthesis]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
RISB_BACAN Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.[HAMAP-Rule:MF_00178][1]
Publication Abstract from PubMed
The crystal structure of lumazine synthase from Bacillus anthracis was solved by molecular replacement and refined to R(cryst) = 23.7% (R(free) = 28.4%) at a resolution of 3.5 A. The structure reveals the icosahedral symmetry of the enzyme and specific features of the active site that are unique in comparison with previously determined orthologues. The application of isothermal titration calorimetry in combination with enzyme kinetics showed that three designed pyrimidine derivatives bind to lumazine synthase with micromolar dissociation constants and competitively inhibit the catalytic reaction. Structure-based modelling suggested the binding modes of the inhibitors in the active site and allowed an estimation of the possible contacts formed upon binding. The results provide a structural framework for the design of antibiotics active against B. anthracis.
Structural study and thermodynamic characterization of inhibitor binding to lumazine synthase from Bacillus anthracis.,Morgunova E, Illarionov B, Saller S, Popov A, Sambaiah T, Bacher A, Cushman M, Fischer M, Ladenstein R Acta Crystallogr D Biol Crystallogr. 2010 Sep;66(Pt 9):1001-11. Epub 2010, Aug 13. PMID:20823551[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Morgunova E, Illarionov B, Saller S, Popov A, Sambaiah T, Bacher A, Cushman M, Fischer M, Ladenstein R. Structural study and thermodynamic characterization of inhibitor binding to lumazine synthase from Bacillus anthracis. Acta Crystallogr D Biol Crystallogr. 2010 Sep;66(Pt 9):1001-11. Epub 2010, Aug 13. PMID:20823551 doi:10.1107/S0907444910029690
- ↑ Morgunova E, Illarionov B, Saller S, Popov A, Sambaiah T, Bacher A, Cushman M, Fischer M, Ladenstein R. Structural study and thermodynamic characterization of inhibitor binding to lumazine synthase from Bacillus anthracis. Acta Crystallogr D Biol Crystallogr. 2010 Sep;66(Pt 9):1001-11. Epub 2010, Aug 13. PMID:20823551 doi:10.1107/S0907444910029690
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