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[[Image:1g57.jpg|left|200px]]


{{Structure
==CRYSTAL STRUCTURE OF 3,4-DIHYDROXY-2-BUTANONE 4-PHOSPHATE SYNTHASE==
|PDB= 1g57 |SIZE=350|CAPTION= <scene name='initialview01'>1g57</scene>, resolution 1.4&Aring;
<StructureSection load='1g57' size='340' side='right'caption='[[1g57]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CS:CESIUM ION'>CS</scene>
<table><tr><td colspan='2'>[[1g57]] 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=1G57 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G57 FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CS:CESIUM+ION'>CS</scene></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=1g57 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g57 OCA], [https://pdbe.org/1g57 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g57 RCSB], [https://www.ebi.ac.uk/pdbsum/1g57 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g57 ProSAT]</span></td></tr>
</table>
== Function ==
[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]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g5/1g57_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1g57 ConSurf].
<div style="clear:both"></div>


'''CRYSTAL STRUCTURE OF 3,4-DIHYDROXY-2-BUTANONE 4-PHOSPHATE SYNTHASE'''
==See Also==
 
*[[Horseradish peroxidase|Horseradish peroxidase]]
 
__TOC__
==Overview==
</StructureSection>
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.
 
==About this Structure==
1G57 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=1G57 OCA].
 
==Reference==
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]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Calabrese, J C.]]
[[Category: Calabrese JC]]
[[Category: Jordan, D B.]]
[[Category: Jordan DB]]
[[Category: Liao, D I.]]
[[Category: Liao D-I]]
[[Category: Viitanen, P V.]]
[[Category: Viitanen PV]]
[[Category: Wawrzak, Z.]]
[[Category: Wawrzak Z]]
[[Category: CS]]
[[Category: antimicrobial target]]
[[Category: dihydroxybutanone phosphate synthase]]
[[Category: riboflavine biosynthesis]]
[[Category: skeletal rearrangement]]
[[Category: structure-based design]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:18:21 2008''

Latest revision as of 07:23, 7 February 2024

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

1g57, resolution 1.40Å

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