3fua: Difference between revisions
New page: left|200px<br /> <applet load="3fua" size="450" color="white" frame="true" align="right" spinBox="true" caption="3fua, resolution 2.67Å" /> '''L-FUCULOSE-1-PHOSPH... |
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==About this Structure== | ==About this Structure== | ||
3FUA 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, CL 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=3FUA OCA]]. | 3FUA 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, CL 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 and PBS. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=3FUA OCA]]. | ||
==Reference== | ==Reference== | ||
Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure., Dreyer MK, Schulz GE, J Mol Biol. 1996 Jun 14;259(3):458-66. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8676381 8676381] | Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure., Dreyer MK, Schulz GE, J Mol Biol. 1996 Jun 14;259(3):458-66. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8676381 8676381] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: L-fuculose-phosphate aldolase]] | |||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Dreyer, M.K.]] | [[Category: Dreyer, M.K.]] | ||
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[[Category: zinc enzyme]] | [[Category: zinc enzyme]] | ||
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Revision as of 14:38, 30 October 2007
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L-FUCULOSE-1-PHOSPHATE ALDOLASE CRYSTAL FORM K
OverviewOverview
The structure of L-fuculose-1-phosphate aldolase in a cubic crystal form, has been determined with and without the inhibitor, phosphoglycolohydroxamate at 2.4 and 2.7 angstrom (1 angstrom = 0.1 nm), resolution, respectively. This inhibitor mimics the enediolate transition, state of the substrate moiety dihydroxyacetone phosphate. The structures, showed that dihydroxyacetone phosphate ligates the zinc ion of this, metal-dependent class II aldolase with its hydroxyl and keto oxygen atoms, shifting Glu73 away from the zinc coordination sphere to a non-polar, environment. At this position Glu73 accepts a proton in the initial, reaction step, producing the enediolate which is then stabilized by the, zinc ion. The other substrate moiety L-lactaldehyde was modeled, because, no binding structure ... [(full description)]
About this StructureAbout this Structure
3FUA is a [Single protein] structure of sequence from [Escherichia coli] with ZN, SO4, CL and BME as [ligands]. Active as [L-fuculose-phosphate aldolase], with EC number [4.1.2.17]. Structure known Active Sites: ACT and PBS. Full crystallographic information is available from [OCA].
ReferenceReference
Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure., Dreyer MK, Schulz GE, J Mol Biol. 1996 Jun 14;259(3):458-66. PMID:8676381
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