1e4b: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1e4b.gif|left|200px]]
-<!--
+==L-Fuculose 1-Phosphate Aldolase from Escherichia coli Mutant N29Q==
-The line below this paragraph, containing "STRUCTURE_1e4b", creates the "Structure Box" on the page.
+<StructureSection load='1e4b' size='340' side='right'caption='[[1e4b]], [[Resolution|resolution]] 1.84&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1e4b]] 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=1E4B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E4B FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.84&#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>
-{{STRUCTURE_1e4b|  PDB=1e4b  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1e4b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e4b OCA], [https://pdbe.org/1e4b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e4b RCSB], [https://www.ebi.ac.uk/pdbsum/1e4b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e4b 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/e4/1e4b_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=1e4b ConSurf].
+<div style="clear:both"></div>
-'''L-FUCULOSE 1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI MUTANT N29Q'''
+==See Also==
+*[[Aldolase 3D structures|Aldolase 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-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 hydroxy ion; the FucA polypeptide does not assume its minimum energy state but oscillates between two states of elevated energy as demonstrated by a mutant in a minimum energy state. The back and forth motion involves a mobile loop connecting the phosphate site with intersubunit motions and thus with the Brownian motion of the solvent. The phosphate group is bound strongly at a given distance to the zinc ion, which prevents the formation of too tight a DHAP:zinc complex. This observation explains our failure to find mutants that accept phosphate-free substitutes for DHAP. The FucA zinc coordination sphere is compared with that of carbonic anhydrase.
-==About this Structure==
-E4B 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=1E4B OCA].
-==Reference==
-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://www.ncbi.nlm.nih.gov/pubmed/11054289 11054289]
 [[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: Bacterial l-fucose metabolism]]
-[[Category: Cleavage of l-fuculose-1-phosphate to dihydroxyacetone phosphate and l-lactaldehyde]]
-[[Category: Mutant structure]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:38:41 2008''