1dzu
From Proteopedia
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| - | [[Image:1dzu. | + | [[Image:1dzu.jpg|left|200px]]<br /><applet load="1dzu" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1dzu" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1dzu, resolution 2.09Å" /> | caption="1dzu, resolution 2.09Å" /> | ||
'''L-FUCULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI MUTANT T26A'''<br /> | '''L-FUCULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI MUTANT T26A'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1DZU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ZN, SO4 and BME as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] | + | 1DZU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ZN, SO4 and BME as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Known structural/functional Sites: <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>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DZU OCA]. |
==Reference== | ==Reference== | ||
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[[Category: mutant structure]] | [[Category: mutant structure]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 14:48:33 2007'' |
Revision as of 12:38, 18 December 2007
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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 with ZN, SO4 and BME as ligands. Active as L-fuculose-phosphate aldolase, with EC number 4.1.2.17 Known structural/functional Sites: , and . 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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