1did
From Proteopedia
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|PDB= 1did |SIZE=350|CAPTION= <scene name='initialview01'>1did</scene>, resolution 2.5Å | |PDB= 1did |SIZE=350|CAPTION= <scene name='initialview01'>1did</scene>, resolution 2.5Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=DIG:2,5-DIDEOXY-2,5-IMINO-D-GLUCITOL'>DIG</scene> | + | |LIGAND= <scene name='pdbligand=DIG:2,5-DIDEOXY-2,5-IMINO-D-GLUCITOL'>DIG</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1did FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1did OCA], [http://www.ebi.ac.uk/pdbsum/1did PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1did RCSB]</span> | ||
}} | }} | ||
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[[Category: Collyer, C A.]] | [[Category: Collyer, C A.]] | ||
[[Category: Goldberg, J D.]] | [[Category: Goldberg, J D.]] | ||
| - | [[Category: DIG]] | ||
| - | [[Category: MN]] | ||
[[Category: isomerase(intramolecular oxidoreductse)]] | [[Category: isomerase(intramolecular oxidoreductse)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:42:05 2008'' |
Revision as of 16:42, 30 March 2008
| |||||||
| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Xylose isomerase, with EC number 5.3.1.5 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
OBSERVATIONS OF REACTION INTERMEDIATES AND THE MECHANISM OF ALDOSE-KETOSE INTERCONVERSION BY D-XYLOSE ISOMERASE
Overview
Crystallographic studies of D-xylose isomerase (D-xylose ketol-isomerase, EC 5.3.1.5) incubated to equilibrium with substrate/product mixtures of xylose and xylulose show electron density for a bound intermediate. The accumulation of this bound intermediate shows that the mechanism is a non-Michaelis type. Carrell et al. [Carrell, H. L., Glusker, J. P., Burger, V., Manfre, F., Tritsch, D. & Biellmann, J.-F. (1989) Proc. Natl. Acad. Sci. USA 86, 4440-4444] and the present authors studied crystals of the enzyme-substrate complex under different conditions and made different interpretations of the substrate density, leading to different conclusions about the enzyme mechanism. All authors agree that the bound intermediate of the sugar is in an open-chain form. It is suggested that the higher-temperature study of Carrell et al. may have produced an equilibrium of multiple states, whose density fits poorly to the open-chain substrate, and led to incorrect interpretation. The two groups also bound different closed-ring sugar analogues to the enzyme, but these analogues bind differently. A possible explanation consistent with all the data is that the enzyme operates by a hydride shift mechanism.
About this Structure
1DID is a Single protein structure of sequence from Arthrobacter sp.. Full crystallographic information is available from OCA.
Reference
Observations of reaction intermediates and the mechanism of aldose-ketose interconversion by D-xylose isomerase., Collyer CA, Blow DM, Proc Natl Acad Sci U S A. 1990 Feb;87(4):1362-6. PMID:2304904
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