1e4c: Difference between revisions

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New page: left|200px<br /> <applet load="1e4c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e4c, resolution 1.66Å" /> '''L-FUCULOSE 1-PHOSPH...
 
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[[Image:1e4c.gif|left|200px]]<br />
<applet load="1e4c" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1e4c, resolution 1.66&Aring;" />
'''L-FUCULOSE 1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI MUTANT S71Q'''<br />


==Overview==
==L-Fuculose 1-Phosphate Aldolase from Escherichia coli Mutant S71Q==
The crystal structures of l-fuculose-1-phosphate aldolase (FucA) with and, without a ligated analogue of dihydroxyacetone phosphate (DHAP) and of a, number of active center mutants have resulted in a model of the catalytic, mechanism. This model has now been confirmed by structural analyses of, further mutations at the zinc coordination sphere and at the phosphate, site. In addition, these mutants have revealed new aspects of the, catalysis: the hydroxyl group of Tyr113' (from a neighboring subunit), which sits just outside the zinc coordination sphere, steers DHAP towards, a productive binding mode at the zinc ion; Glu73 contacts zinc in between, the two ligand positions intended for the DHAP oxygen atoms and thus, avoids blocking of these positions by a tetrahedrally coordinated ... [[http://ispc.weizmann.ac.il/pmbin/getpm?11054289 (full description)]]
<StructureSection load='1e4c' size='340' side='right'caption='[[1e4c]], [[Resolution|resolution]] 1.66&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1e4c]] is a 1 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=1E4C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E4C 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]] 1.66&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1e4c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e4c OCA], [https://pdbe.org/1e4c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e4c RCSB], [https://www.ebi.ac.uk/pdbsum/1e4c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e4c ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FUCA_ECOLI FUCA_ECOLI]
== 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/e4/1e4c_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=1e4c ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1E4C 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 SO4, ZN and BME as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.17 4.1.2.17]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E4C OCA]].
*[[Aldolase 3D structures|Aldolase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Structures of l-fuculose-1-phosphate aldolase mutants outlining motions during catalysis., Joerger AC, Mueller-Dieckmann C, Schulz GE, J Mol Biol. 2000 Nov 3;303(4):531-43. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11054289 11054289]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Joerger, A.C.]]
[[Category: Joerger AC]]
[[Category: Schulz, G.E.]]
[[Category: Schulz GE]]
[[Category: BME]]
[[Category: SO4]]
[[Category: ZN]]
[[Category: aldolase (class ii)]]
[[Category: bacterial l-fucose metabolism]]
[[Category: cleavage of l-fuculose-1-phosphate to dihydroxyacetone phosphate and l-lactaldehyde]]
[[Category: mutant structure]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 15:48:21 2007''

Latest revision as of 12:58, 20 March 2024

L-Fuculose 1-Phosphate Aldolase from Escherichia coli Mutant S71QL-Fuculose 1-Phosphate Aldolase from Escherichia coli Mutant S71Q

Structural highlights

1e4c is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.66Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FUCA_ECOLI

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1e4c, resolution 1.66Å

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