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[[Image:1e4a.gif|left|200px]]<br />
<applet load="1e4a" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1e4a, resolution 2.15&Aring;" />
'''L-FUCULOSE 1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI MUTANT DEL(27)'''<br />


==Overview==
==L-Fuculose 1-Phosphate Aldolase from Escherichia coli Mutant Del(27)==
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='1e4a' size='340' side='right'caption='[[1e4a]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1e4a]] 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=1E4A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E4A 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]] 2.15&#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=1e4a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e4a OCA], [https://pdbe.org/1e4a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e4a RCSB], [https://www.ebi.ac.uk/pdbsum/1e4a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e4a 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/e4/1e4a_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=1e4a ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1E4A 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/L-fuculose-phosphate_aldolase L-fuculose-phosphate aldolase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.17 4.1.2.17]]. Structure known Active Sites: ACT and MUT. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E4A 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: L-fuculose-phosphate aldolase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Joerger AC]]
[[Category: Joerger, A.C.]]
[[Category: Schulz GE]]
[[Category: Schulz, G.E.]]
[[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 Tue Oct 30 10:01:32 2007''

Latest revision as of 12:58, 20 March 2024

L-Fuculose 1-Phosphate Aldolase from Escherichia coli Mutant Del(27)L-Fuculose 1-Phosphate Aldolase from Escherichia coli Mutant Del(27)

Structural highlights

1e4a 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 2.15Å
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

1e4a, resolution 2.15Å

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