1xlm: Difference between revisions
New page: left|200px<br /> <applet load="1xlm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xlm, resolution 2.4Å" /> '''D254E, D256E MUTANT ... |
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==About this Structure== | ==About this Structure== | ||
1XLM is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Arthrobacter_sp. Arthrobacter sp.]] with XYL and AL 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=5.3.1.5 5.3.1.5]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XLM OCA]]. | 1XLM is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Arthrobacter_sp. Arthrobacter sp.]] with XYL and AL as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Xylose_isomerase Xylose isomerase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.5 5.3.1.5]]. Structure known Active Sites: CTA and CTB. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XLM OCA]]. | ||
==Reference== | ==Reference== | ||
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[[Category: Arthrobacter sp.]] | [[Category: Arthrobacter sp.]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Xylose isomerase]] | |||
[[Category: Asboth, B.]] | [[Category: Asboth, B.]] | ||
[[Category: Bocskei, Z.S.]] | [[Category: Bocskei, Z.S.]] | ||
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[[Category: xylose metabolism]] | [[Category: xylose metabolism]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:21:21 2007'' | ||
Revision as of 14:16, 30 October 2007
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D254E, D256E MUTANT OF D-XYLOSE ISOMERASE COMPLEXED WITH AL3 AND XYLITOL
OverviewOverview
The active site and mechanism of D-xylose isomerase have been probed by, determination of the crystal structures of the enzyme bound to various, substrates, inhibitors and cations. Ring-opening is an obligatory first, step of the reaction and is believed to be the rate-determining step for, the aldose to ketose conversion. The structure of a complex with a cyclic, thio-glucose has been determined and it is concluded that this is an, analogue of the Michaelis complex. At -10 degrees C substrates in crystals, are observed in the extended chain form. The absence of an appropriately, situated base for either the cyclic or extended chain forms from the, substrate binding site indicates that the isomerisation does not take, place by an enediol or enediolate mechanism. Binding of a trivalent ... [(full description)]
About this StructureAbout this Structure
1XLM is a [Single protein] structure of sequence from [Arthrobacter sp.] with XYL and AL as [ligands]. Active as [Xylose isomerase], with EC number [5.3.1.5]. Structure known Active Sites: CTA and CTB. Full crystallographic information is available from [OCA].
ReferenceReference
Mechanism for aldose-ketose interconversion by D-xylose isomerase involving ring opening followed by a 1,2-hydride shift., Collyer CA, Henrick K, Blow DM, J Mol Biol. 1990 Mar 5;212(1):211-35. PMID:2319597
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