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1iez

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[[Image:1iez.gif|left|200px]]
 
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{{Structure
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==Solution Structure of 3,4-Dihydroxy-2-Butanone 4-Phosphate Synthase of Riboflavin Biosynthesis==
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|PDB= 1iez |SIZE=350|CAPTION= <scene name='initialview01'>1iez</scene>
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<StructureSection load='1iez' size='340' side='right'caption='[[1iez]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1iez]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IEZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IEZ FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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|GENE=
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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=1iez FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iez OCA], [https://pdbe.org/1iez PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iez RCSB], [https://www.ebi.ac.uk/pdbsum/1iez PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iez ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=[[1g57|1G57]], [[1g58|1G58]]
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1iez FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iez OCA], [http://www.ebi.ac.uk/pdbsum/1iez PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1iez RCSB]</span>
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[https://www.uniprot.org/uniprot/RIBB_ECOLI RIBB_ECOLI] Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.[HAMAP-Rule:MF_00180]
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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'''Solution Structure of 3,4-Dihydroxy-2-Butanone 4-Phosphate Synthase of Riboflavin Biosynthesis'''
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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/ie/1iez_consurf.spt"</scriptWhenChecked>
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==Overview==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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Recent developments in NMR have extended the size range of proteins amenable to structural and functional characterization to include many larger proteins involved in important cellular processes. By applying a combination of residue-specific isotope labeling and protein deuteration strategies tailored to yield specific information, we were able to determine the solution structure and study structure-activity relationships of 3,4-dihydroxy-2-butanone-4-phosphate synthase, a 47-kDa enzyme from the Escherichia coli riboflavin biosynthesis pathway and an attractive target for novel antibiotics. Our investigations of the enzyme's ligand binding by NMR and site-directed mutagenesis yields a conclusive picture of the location and identity of residues directly involved in substrate binding and catalysis. Our studies illustrate the power of state-of-the-art NMR techniques for the structural characterization and investigation of ligand binding in protein complexes approaching the 50-kDa range in solution.
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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==About this Structure==
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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=1iez ConSurf].
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1IEZ 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=1IEZ OCA].
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<div style="clear:both"></div>
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__TOC__
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==Reference==
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</StructureSection>
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The NMR structure of the 47-kDa dimeric enzyme 3,4-dihydroxy-2-butanone-4-phosphate synthase and ligand binding studies reveal the location of the active site., Kelly MJ, Ball LJ, Krieger C, Yu Y, Fischer M, Schiffmann S, Schmieder P, Kuhne R, Bermel W, Bacher A, Richter G, Oschkinat H, Proc Natl Acad Sci U S A. 2001 Nov 6;98(23):13025-30. Epub 2001 Oct 30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11687623 11687623]
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[[Category: Escherichia coli K-12]]
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[[Category: Escherichia coli]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Bacher A]]
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[[Category: Bacher, A.]]
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[[Category: Ball LJ]]
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[[Category: Ball, L J.]]
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[[Category: Kelly MJS]]
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[[Category: Kelly, M J.S.]]
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[[Category: Kuhne R]]
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[[Category: Kuhne, R.]]
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[[Category: Oschkinat H]]
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[[Category: Oschkinat, H.]]
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[[Category: antimicrobial target]]
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[[Category: dihydroxybutanone phosphate synthase]]
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[[Category: riboflavin biosynthesis]]
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[[Category: skeletal rearrangement]]
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[[Category: structure based design]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:18:52 2008''
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Current revision

Solution Structure of 3,4-Dihydroxy-2-Butanone 4-Phosphate Synthase of Riboflavin Biosynthesis

PDB ID 1iez

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