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| - | [[Image:1i8d.gif|left|200px]] | |
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| - | {{Structure
| + | ==CRYSTAL STRUCTURE OF RIBOFLAVIN SYNTHASE== |
| - | |PDB= 1i8d |SIZE=350|CAPTION= <scene name='initialview01'>1i8d</scene>, resolution 2.0Å
| + | <StructureSection load='1i8d' size='340' side='right'caption='[[1i8d]], [[Resolution|resolution]] 2.00Å' scene=''> |
| - | |SITE=
| + | == Structural highlights == |
| - | |LIGAND=
| + | <table><tr><td colspan='2'>[[1i8d]] 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=1I8D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I8D FirstGlance]. <br> |
| - | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Riboflavin_synthase Riboflavin synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.9 2.5.1.9] </span>
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | |GENE= BACTERIA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1i8d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i8d OCA], [https://pdbe.org/1i8d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i8d RCSB], [https://www.ebi.ac.uk/pdbsum/1i8d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i8d ProSAT]</span></td></tr> |
| - | |DOMAIN=
| + | </table> |
| - | |RELATEDENTRY=
| + | == Function == |
| - | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1i8d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i8d OCA], [http://www.ebi.ac.uk/pdbsum/1i8d PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1i8d RCSB]</span>
| + | [https://www.uniprot.org/uniprot/RISA_ECOLI RISA_ECOLI] Catalyzes the dismutation of two molecules of 6,7-dimethyl-8-ribityllumazine, resulting in the formation of riboflavin and 5-amino-6-(D-ribitylamino)uracil. |
| - | }}
| + | == Evolutionary Conservation == |
| - | | + | [[Image:Consurf_key_small.gif|200px|right]] |
| - | '''CRYSTAL STRUCTURE OF RIBOFLAVIN SYNTHASE'''
| + | Check<jmol> |
| - | | + | <jmolCheckbox> |
| - | | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i8/1i8d_consurf.spt"</scriptWhenChecked> |
| - | ==Overview== | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| - | BACKGROUND: Riboflavin synthase catalyzes the dismutation of two molecules of 6,7-dimethyl-8-(1'-D-ribityl)-lumazine to yield riboflavin and 4-ribitylamino-5-amino-2,6-dihydroxypyrimidine. The homotrimer of 23 kDa subunits has no cofactor requirements for catalysis. The enzyme is nonexistent in humans and is an attractive target for antimicrobial agents of organisms whose pathogenicity depends on their ability to biosynthesize riboflavin. RESULTS: The first three-dimensional structure of the enzyme was determined at 2.0 A resolution using the multiwavelength anomalous diffraction (MAD) method on the Escherichia coli protein containing selenomethionine residues. The homotrimer consists of an asymmetric assembly of monomers, each of which comprises two similar beta barrels and a C-terminal alpha helix. The similar beta barrels within the monomer confirm a prediction of pseudo two-fold symmetry that is inferred from the sequence similarity between the two halves of the protein. The beta barrels closely resemble folds found in phthalate dioxygenase reductase and other flavoproteins. CONCLUSIONS: The three active sites of the trimer are proposed to lie between pairs of monomers in which residues conserved among species reside, including two Asp-His-Ser triads and dyads of Cys-Ser and His-Thr. The proposed active sites are located where FMN (an analog of riboflavin) is modeled from an overlay of the beta barrels of phthalate dioxygenase reductase and riboflavin synthase. In the trimer, one active site is formed, and the other two active sites are wide open and exposed to solvent. The nature of the trimer configuration suggests that only one active site can be formed and be catalytically competent at a time.
| + | <text>to colour the structure by Evolutionary Conservation</text> |
| - | | + | </jmolCheckbox> |
| - | ==About this Structure== | + | </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=1i8d ConSurf]. |
| - | 1I8D 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=1I8D OCA].
| + | <div style="clear:both"></div> |
| - | | + | __TOC__ |
| - | ==Reference== | + | </StructureSection> |
| - | Crystal structure of riboflavin synthase., Liao DI, Wawrzak Z, Calabrese JC, Viitanen PV, Jordan DB, Structure. 2001 May 9;9(5):399-408. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11377200 11377200]
| + | |
| | [[Category: Escherichia coli]] | | [[Category: Escherichia coli]] |
| - | [[Category: Riboflavin synthase]] | + | [[Category: Large Structures]] |
| - | [[Category: Single protein]]
| + | [[Category: Calabrese JC]] |
| - | [[Category: Calabrese, J C.]] | + | [[Category: Jordan DB]] |
| - | [[Category: Jordan, D B.]] | + | [[Category: Liao D-I]] |
| - | [[Category: Liao, D I.]] | + | [[Category: Viitanen PV]] |
| - | [[Category: Viitanen, P V.]] | + | [[Category: Wawrzak Z]] |
| - | [[Category: Wawrzak, Z.]] | + | |
| - | [[Category: antimicrobial target]]
| + | |
| - | [[Category: escherichia coli]]
| + | |
| - | [[Category: riboflavin biosynthesis]]
| + | |
| - | [[Category: riboflavin synthase]]
| + | |
| - | [[Category: structure-based design]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:16:03 2008''
| + | |
