1dzz: Difference between revisions
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|PDB= 1dzz |SIZE=350|CAPTION= <scene name='initialview01'>1dzz</scene>, resolution 1.92Å | |PDB= 1dzz |SIZE=350|CAPTION= <scene name='initialview01'>1dzz</scene>, resolution 1.92Å | ||
|SITE= <scene name='pdbsite=ACT:Active+Center+Definded+By+The+Zn+Ion+And+The+Four+Zn+Coo+...'>ACT</scene>, <scene name='pdbsite=MUT:Mutation+Site'>MUT</scene> and <scene name='pdbsite=PBS:The+Substrate+Phosphate+Binding+Site+Near+The+Active+Cen+...'>PBS</scene> | |SITE= <scene name='pdbsite=ACT:Active+Center+Definded+By+The+Zn+Ion+And+The+Four+Zn+Coo+...'>ACT</scene>, <scene name='pdbsite=MUT:Mutation+Site'>MUT</scene> and <scene name='pdbsite=PBS:The+Substrate+Phosphate+Binding+Site+Near+The+Active+Cen+...'>PBS</scene> | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</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=1dzz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dzz OCA], [http://www.ebi.ac.uk/pdbsum/1dzz PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dzz RCSB]</span> | |||
}} | }} | ||
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[[Category: Joerger, A C.]] | [[Category: Joerger, A C.]] | ||
[[Category: Schulz, G E.]] | [[Category: Schulz, G E.]] | ||
[[Category: aldolase (class ii)]] | [[Category: aldolase (class ii)]] | ||
[[Category: bacterial l-fucose metabolism]] | [[Category: bacterial l-fucose metabolism]] | ||
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[[Category: mutant structure]] | [[Category: mutant structure]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:52:20 2008'' | ||
Revision as of 16:52, 30 March 2008
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| 1dzz, resolution 1.92Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Sites: | ACT, MUT and PBS | ||||||||||||
| Ligands: | BME, SO4, ZN | ||||||||||||
| 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 FROM ESCHERICHIA COLI MUTANT Y113F
Overview
Previous analyses established the structures of unligated L-fuculose 1-phosphate aldolase and of the enzyme ligated with an inhibitor mimicking the substrate dihydroxyacetone phosphate. These data allowed us to suggest a catalytic mechanism. On the basis of this proposal, numerous mutations were now introduced at the active center and tested with respect to their catalytic rates and their product distributions. For several mutants, the structures were determined. The results demonstrate the catalytic importance of some particular residues in defined conformations and in the mobile C-terminal chain end. Moreover, they led to a modification of the proposed mechanism. The effect of some mutations on enantioselectivity and on the ratio of diastereomer formation indicates clearly the binding site of the aldehyde moiety in relation to the other substrate dihydroxyacetone phosphate.
About this Structure
1DZZ is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Catalytic action of fuculose 1-phosphate aldolase (class II) as derived from structure-directed mutagenesis., Joerger AC, Gosse C, Fessner WD, Schulz GE, Biochemistry. 2000 May 23;39(20):6033-41. PMID:10821675
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