1dzu
From Proteopedia
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| - | [[Image:1dzu.jpg|left|200px]] | + | [[Image:1dzu.jpg|left|200px]] |
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| - | '''L-FUCULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI MUTANT T26A''' | + | {{Structure |
| + | |PDB= 1dzu |SIZE=350|CAPTION= <scene name='initialview01'>1dzu</scene>, resolution 2.09Å | ||
| + | |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=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</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 FROM ESCHERICHIA COLI MUTANT T26A''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1DZU is a [ | + | 1DZU 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=1DZU OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10821675 10821675] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: L-fuculose-phosphate aldolase]] | [[Category: L-fuculose-phosphate aldolase]] | ||
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[[Category: mutant structure]] | [[Category: mutant structure]] | ||
| - | ''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 10:47:08 2008'' |
Revision as of 08:47, 20 March 2008
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| , resolution 2.09Å | |||||||
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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 FROM ESCHERICHIA COLI MUTANT T26A
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
1DZU 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
Page seeded by OCA on Thu Mar 20 10:47:08 2008
