1e46: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1e46]] is a 1 chain structure with 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=1E46 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E46 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1e46]] is a 1 chain structure with 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=1E46 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E46 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3fua|3fua]], [[2fua|2fua]], [[1fua|1fua]], [[1dzy|1dzy]], [[1dzz|1dzz]], [[1dzu|1dzu]], [[1dzv|1dzv]], [[1dzw|1dzw]], [[1dzx|1dzx]], [[4fua|4fua]], [[1e47|1e47]], [[1e48|1e48]], [[1e49|1e49]], [[1e4a|1e4a]], [[1e4b|1e4b]], [[1e4c|1e4c]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3fua|3fua]], [[2fua|2fua]], [[1fua|1fua]], [[1dzy|1dzy]], [[1dzz|1dzz]], [[1dzu|1dzu]], [[1dzv|1dzv]], [[1dzw|1dzw]], [[1dzx|1dzx]], [[4fua|4fua]], [[1e47|1e47]], [[1e48|1e48]], [[1e49|1e49]], [[1e4a|1e4a]], [[1e4b|1e4b]], [[1e4c|1e4c]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e46 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e46 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1e46 RCSB], [http://www.ebi.ac.uk/pdbsum/1e46 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e46 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e46 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1e46 RCSB], [http://www.ebi.ac.uk/pdbsum/1e46 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 35: | Line 35: | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: L-fuculose-phosphate aldolase]] | [[Category: L-fuculose-phosphate aldolase]] | ||
[[Category: Joerger, A C | [[Category: Joerger, A C]] | ||
[[Category: Schulz, G E | [[Category: Schulz, G E]] | ||
[[Category: Bacterial l-fucose metabolism]] | [[Category: Bacterial l-fucose metabolism]] | ||
[[Category: Cleavage of l-fuculose 1-phosphate to dihydroxyacetone phosphate and l-lactaldehyde]] | [[Category: Cleavage of l-fuculose 1-phosphate to dihydroxyacetone phosphate and l-lactaldehyde]] | ||
[[Category: Mutant structure]] | [[Category: Mutant structure]] | ||
Revision as of 01:01, 23 December 2014
L-FUCULOSE 1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI MUTANT E73SL-FUCULOSE 1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI MUTANT E73S
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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:11054289[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||||