3fua: Difference between revisions
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[[Image:3fua. | [[Image:3fua.jpg|left|200px]]<br /><applet load="3fua" size="450" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="3fua" size="450" color="white" frame="true" align="right" spinBox="true" | |||
caption="3fua, resolution 2.67Å" /> | caption="3fua, resolution 2.67Å" /> | ||
'''L-FUCULOSE-1-PHOSPHATE ALDOLASE CRYSTAL FORM K'''<br /> | '''L-FUCULOSE-1-PHOSPHATE ALDOLASE CRYSTAL FORM K'''<br /> | ||
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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/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] | 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] Known structural/functional Sites: <scene name='pdbsite=ACT:The Active Center Is Defined By The Zn Ion, The Four Zn ...'>ACT</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=3FUA OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: zinc enzyme]] | [[Category: zinc enzyme]] | ||
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Revision as of 21:29, 18 December 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 is yet available.
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 Known structural/functional Sites: and . 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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