1g58

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[[Image:1g58.jpg|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF 3,4-DIHYDROXY-2-BUTANONE 4-PHOSPHATE SYNTHASE GOLD DERIVATIVE==
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|PDB= 1g58 |SIZE=350|CAPTION= <scene name='initialview01'>1g58</scene>, resolution 1.55&Aring;
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<StructureSection load='1g58' size='340' side='right'caption='[[1g58]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=AU:GOLD+ION'>AU</scene>
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<table><tr><td colspan='2'>[[1g58]] is a 2 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=1G58 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G58 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">X-ray diffraction, [[Resolution|Resolution]] 1.55&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AU:GOLD+ION'>AU</scene></td></tr>
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|DOMAIN=
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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=1g58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g58 OCA], [https://pdbe.org/1g58 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g58 RCSB], [https://www.ebi.ac.uk/pdbsum/1g58 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g58 ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g58 OCA], [http://www.ebi.ac.uk/pdbsum/1g58 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1g58 RCSB]</span>
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== Function ==
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}}
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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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== Evolutionary Conservation ==
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'''CRYSTAL STRUCTURE OF 3,4-DIHYDROXY-2-BUTANONE 4-PHOSPHATE SYNTHASE GOLD DERIVATIVE'''
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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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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g5/1g58_consurf.spt"</scriptWhenChecked>
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BACKGROUND: 3,4-Dihydroxy-2-butanone-4-phosphate synthase catalyzes a commitment step in the biosynthesis of riboflavin. On the enzyme, ribulose 5-phosphate is converted to 3,4-dihydroxy-2-butanone 4-phosphate and formate in steps involving enolization, ketonization, dehydration, skeleton rearrangement, and formate elimination. The enzyme is absent in humans and an attractive target for the discovery of antimicrobials for pathogens incapable of acquiring sufficient riboflavin from their hosts. The homodimer of 23 kDa subunits requires Mg(2+) for activity. RESULTS: The first three-dimensional structure of the enzyme was determined at 1.4 A resolution using the multiwavelength anomalous diffraction (MAD) method on Escherichia coli protein crystals containing gold. The protein consists of an alpha + beta fold having a complex linkage of beta strands. Intersubunit contacts are mediated by numerous hydrophobic interactions and three hydrogen bond networks. CONCLUSIONS: A proposed active site was identified on the basis of amino acid residues that are conserved among the enzyme from 19 species. There are two well-separated active sites per dimer, each of which comprise residues from both subunits. In addition to three arginines and two threonines, which may be used for recognizing the phosphate group of the substrate, the active site consists of three glutamates, two aspartates, two histidines, and a cysteine which may provide the means for general acid and base catalysis and for coordinating the Mg(2+) cofactor within the active site.
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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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==About this Structure==
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</jmolCheckbox>
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1G58 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=1G58 OCA].
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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=1g58 ConSurf].
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<div style="clear:both"></div>
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==Reference==
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__TOC__
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Crystal structure of 3,4-dihydroxy-2-butanone 4-phosphate synthase of riboflavin biosynthesis., Liao DI, Calabrese JC, Wawrzak Z, Viitanen PV, Jordan DB, Structure. 2001 Jan 10;9(1):11-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11342130 11342130]
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Calabrese, J C.]]
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[[Category: Calabrese JC]]
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[[Category: Jordan, D B.]]
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[[Category: Jordan DB]]
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[[Category: Liao, D I.]]
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[[Category: Liao D-I]]
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[[Category: Viitanen, P V.]]
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[[Category: Viitanen PV]]
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[[Category: Wawrzak, Z.]]
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[[Category: Wawrzak Z]]
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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 20:36:52 2008''
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Current revision

CRYSTAL STRUCTURE OF 3,4-DIHYDROXY-2-BUTANONE 4-PHOSPHATE SYNTHASE GOLD DERIVATIVE

PDB ID 1g58

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