4fua
From Proteopedia
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| - | [[Image:4fua.jpg|left|200px]] | + | [[Image:4fua.jpg|left|200px]] |
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| - | '''L-FUCULOSE-1-PHOSPHATE ALDOLASE COMPLEX WITH PGH''' | + | {{Structure |
| + | |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> | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene> and <scene name='pdbligand=PGH:PHOSPHOGLYCOLOHYDROXAMIC ACID'>PGH</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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''L-FUCULOSE-1-PHOSPHATE ALDOLASE COMPLEX WITH PGH''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 4FUA is a [ | + | 4FUA 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=4FUA OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8676381 8676381] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: L-fuculose-phosphate aldolase]] | [[Category: L-fuculose-phosphate aldolase]] | ||
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[[Category: zinc enzyme]] | [[Category: zinc enzyme]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:09:41 2008'' |
Revision as of 17:09, 20 March 2008
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| , resolution 2.43Å | |||||||
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| Sites: | and | ||||||
| Ligands: | , , and | ||||||
| Activity: | L-fuculose-phosphate aldolase, with EC number 4.1.2.17 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
L-FUCULOSE-1-PHOSPHATE ALDOLASE COMPLEX WITH PGH
Overview
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 Structure
4FUA is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 19:09:41 2008
