1dzz

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(New page: 200px<br /> <applet load="1dzz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dzz, resolution 1.92&Aring;" /> '''L-FUCULOSE-1-PHOSPH...)
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==About this Structure==
==About this Structure==
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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/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.17 4.1.2.17]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DZZ OCA]].
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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]]. Structure known Active Sites: ACT, MUT and PBS. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DZZ 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://ispc.weizmann.ac.il//pmbin/getpm?pmid=10821675 10821675]
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=10821675 10821675]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: L-fuculose-phosphate aldolase]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Joerger, A.C.]]
[[Category: Joerger, A.C.]]
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[[Category: mutant structure]]
[[Category: mutant structure]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 17:11:29 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:01:41 2007''

Revision as of 08:56, 30 October 2007


1dzz, resolution 1.92Å

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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 ... [(full description)]

About this Structure

1DZZ 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]. Structure known Active Sites: ACT, MUT and PBS. 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 Tue Oct 30 11:01:41 2007

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