1dzz: Difference between revisions

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[[Image:1dzz.jpg|left|200px]]<br /><applet load="1dzz" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1dzz.jpg|left|200px]]<br /><applet load="1dzz" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1dzz, resolution 1.92&Aring;" />
caption="1dzz, resolution 1.92&Aring;" />
'''L-FUCULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI MUTANT Y113F'''<br />
'''L-FUCULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI MUTANT Y113F'''<br />
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==About this Structure==
==About this Structure==
1DZZ 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=1DZZ OCA].  
1DZZ 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 <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=BME:'>BME</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1DZZ OCA].  


==Reference==
==Reference==
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[[Category: mutant structure]]
[[Category: mutant structure]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 14:49:46 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:36:22 2008''

Revision as of 10:36, 3 February 2008

File:1dzz.jpg


1dzz, resolution 1.92Å

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L-FUCULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI MUTANT Y113F

OverviewOverview

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 StructureAbout this Structure

1DZZ is a Single protein structure of sequence from Escherichia coli with , and 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.

ReferenceReference

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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