4fua: Difference between revisions
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|PDB= 4fua |SIZE=350|CAPTION= <scene name='initialview01'>4fua</scene>, resolution 2.43Å | |PDB= 4fua |SIZE=350|CAPTION= <scene name='initialview01'>4fua</scene>, resolution 2.43Å | ||
|SITE= <scene name='pdbsite=ACT:The+Active+Center+Is+Defined+By+The+Zn+Ion,+The+Four+Zn+...'>ACT</scene> and <scene name='pdbsite=PBS:Binding+Site+For+The+Substrate+Phosphate+Group'>PBS</scene> | |SITE= <scene name='pdbsite=ACT:The+Active+Center+Is+Defined+By+The+Zn+Ion,+The+Four+Zn+...'>ACT</scene> and <scene name='pdbsite=PBS:Binding+Site+For+The+Substrate+Phosphate+Group'>PBS</scene> | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=PGH:PHOSPHOGLYCOLOHYDROXAMIC+ACID'>PGH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> | ||
|ACTIVITY= [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] | |ACTIVITY= <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> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fua FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fua OCA], [http://www.ebi.ac.uk/pdbsum/4fua PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=4fua RCSB]</span> | |||
}} | }} | ||
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[[Category: Dreyer, M K.]] | [[Category: Dreyer, M K.]] | ||
[[Category: Schulz, G E.]] | [[Category: Schulz, G E.]] | ||
[[Category: class ii aldolase]] | [[Category: class ii aldolase]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
[[Category: zinc enzyme]] | [[Category: zinc enzyme]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:38:46 2008'' | ||
Revision as of 05:38, 31 March 2008
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| , resolution 2.43Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | and | ||||||
| Ligands: | , , , | ||||||
| Activity: | L-fuculose-phosphate aldolase, with EC number 4.1.2.17 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
L-FUCULOSE-1-PHOSPHATE ALDOLASE COMPLEX WITH PGH
OverviewOverview
The structure of L-fuculose-1-phosphate aldolase in a cubic crystal form has been determined with and without the inhibitor phosphoglycolohydroxamate at 2.4 and 2.7 angstrom (1 angstrom = 0.1 nm) resolution, respectively. This inhibitor mimics the enediolate transition state of the substrate moiety dihydroxyacetone phosphate. The structures showed that dihydroxyacetone phosphate ligates the zinc ion of this metal-dependent class II aldolase with its hydroxyl and keto oxygen atoms, shifting Glu73 away from the zinc coordination sphere to a non-polar environment. At this position Glu73 accepts a proton in the initial reaction step, producing the enediolate which is then stabilized by the zinc ion. The other substrate moiety L-lactaldehyde was modeled, because no binding structure is yet available.
About this StructureAbout this Structure
4FUA is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure., Dreyer MK, Schulz GE, J Mol Biol. 1996 Jun 14;259(3):458-66. PMID:8676381
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