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New page: left|200px<br /><applet load="1iho" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iho, resolution 1.70Å" /> '''CRYSTAL APO-STRUCTUR...
 
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[[Image:1iho.gif|left|200px]]<br /><applet load="1iho" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1iho, resolution 1.70&Aring;" />
'''CRYSTAL APO-STRUCTURE OF PANTOTHENATE SYNTHETASE FROM E. COLI'''<br />


==Overview==
==CRYSTAL APO-STRUCTURE OF PANTOTHENATE SYNTHETASE FROM E. COLI==
BACKGROUND: Pantothenate synthetase (EC 6.3.2.1) is the last enzyme of the, pathway of pantothenate (vitamin B(5)) synthesis. It catalyzes the, condensation of pantoate with beta-alanine in an ATP-dependent reaction., RESULTS: We describe the overexpression, purification, and crystal, structure of recombinant pantothenate synthetase from E. coli. The, structure was solved by a selenomethionine multiwavelength anomalous, dispersion experiment and refined against native data to a final R(cryst), of 22.6% (R(free) = 24.9%) at 1.7 A resolution. The enzyme is dimeric, with two well-defined domains per protomer: the N-terminal domain, a, Rossmann fold, contains the active site cavity, with the C-terminal domain, forming a hinged lid. CONCLUSIONS: The N-terminal domain is structurally, very similar to class I aminoacyl-tRNA synthetases and is thus a member of, the cytidylyltransferase superfamily. This relationship has been used to, suggest the location of the ATP and pantoate binding sites and the nature, of hinge bending that leads to the ternary enzyme-pantoate-ATP complex.
<StructureSection load='1iho' size='340' side='right'caption='[[1iho]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1iho]] 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=1IHO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IHO FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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=1iho FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iho OCA], [https://pdbe.org/1iho PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iho RCSB], [https://www.ebi.ac.uk/pdbsum/1iho PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iho ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PANC_ECOLI PANC_ECOLI] Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.<ref>PMID:357689</ref>
== 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/ih/1iho_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=1iho ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1IHO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with TRS and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Pantoate--beta-alanine_ligase Pantoate--beta-alanine ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.1 6.3.2.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IHO OCA].
*[[Pantothenate synthetase|Pantothenate synthetase]]
 
== References ==
==Reference==
<references/>
The crystal structure of E. coli pantothenate synthetase confirms it as a member of the cytidylyltransferase superfamily., von Delft F, Lewendon A, Dhanaraj V, Blundell TL, Abell C, Smith AG, Structure. 2001 May 9;9(5):439-50. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11377204 11377204]
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Pantoate--beta-alanine ligase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Abell C]]
[[Category: Abell, C.]]
[[Category: Blundell TL]]
[[Category: Blundell, T.L.]]
[[Category: Dhanaraj V]]
[[Category: Delft, F.von.]]
[[Category: Lewendon A]]
[[Category: Dhanaraj, V.]]
[[Category: Smith A]]
[[Category: Lewendon, A.]]
[[Category: Von Delft F]]
[[Category: Smith, A.]]
[[Category: EDO]]
[[Category: TRS]]
[[Category: apo]]
[[Category: dimer]]
[[Category: flexible domains]]
[[Category: high]]
[[Category: ksmks]]
[[Category: multidomain]]
[[Category: rossman fold]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:24:09 2007''

Latest revision as of 07:35, 7 February 2024

CRYSTAL APO-STRUCTURE OF PANTOTHENATE SYNTHETASE FROM E. COLI

1iho, resolution 1.70Å

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