2cd9
From Proteopedia
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| - | [[Image:2cd9.gif|left|200px]] | + | [[Image:2cd9.gif|left|200px]] |
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| - | '''SULFOLOBUS SOLFATARICUS GLUCOSE DEHYDROGENASE 1- APO FORM''' | + | {{Structure |
| + | |PDB= 2cd9 |SIZE=350|CAPTION= <scene name='initialview01'>2cd9</scene>, resolution 1.800Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Zn+Binding+Site+For+Chain+B'>AC1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Glucose_1-dehydrogenase Glucose 1-dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.47 1.1.1.47] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''SULFOLOBUS SOLFATARICUS GLUCOSE DEHYDROGENASE 1- APO FORM''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2CD9 is a [ | + | 2CD9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CD9 OCA]. |
==Reference== | ==Reference== | ||
| - | The structural basis of substrate promiscuity in glucose dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus., Milburn CC, Lamble HJ, Theodossis A, Bull SD, Hough DW, Danson MJ, Taylor GL, J Biol Chem. 2006 May 26;281(21):14796-804. Epub 2006 Mar 23. PMID:[http:// | + | The structural basis of substrate promiscuity in glucose dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus., Milburn CC, Lamble HJ, Theodossis A, Bull SD, Hough DW, Danson MJ, Taylor GL, J Biol Chem. 2006 May 26;281(21):14796-804. Epub 2006 Mar 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16556607 16556607] |
[[Category: Glucose 1-dehydrogenase]] | [[Category: Glucose 1-dehydrogenase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:13:58 2008'' |
Revision as of 14:14, 20 March 2008
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| , resolution 1.800Å | |||||||
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| Sites: | |||||||
| Ligands: | |||||||
| Activity: | Glucose 1-dehydrogenase, with EC number 1.1.1.47 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
SULFOLOBUS SOLFATARICUS GLUCOSE DEHYDROGENASE 1- APO FORM
Overview
The hyperthermophilic archaeon Sulfolobus solfataricus grows optimally above 80 degrees C and utilizes an unusual, promiscuous, non-phosphorylative Entner-Doudoroff pathway to metabolize both glucose and galactose. The first enzyme in this pathway, glucose dehydrogenase, catalyzes the oxidation of glucose to gluconate, but has been shown to have activity with a broad range of sugar substrates, including glucose, galactose, xylose, and L-arabinose, with a requirement for the glucose stereo configuration at the C2 and C3 positions. Here we report the crystal structure of the apo form of glucose dehydrogenase to a resolution of 1.8 A and a complex with its required cofactor, NADP+, to a resolution of 2.3 A. A T41A mutation was engineered to enable the trapping of substrate in the crystal. Complexes of the enzyme with D-glucose and D-xylose are presented to resolutions of 1.6 and 1.5 A, respectively, that provide evidence of selectivity for the beta-anomeric, pyranose form of the substrate, and indicate that this is the productive substrate form. The nature of the promiscuity of glucose dehydrogenase is also elucidated, and a physiological role for this enzyme in xylose metabolism is suggested. Finally, the structure suggests that the mechanism of sugar oxidation by this enzyme may be similar to that described for human sorbitol dehydrogenase.
About this Structure
2CD9 is a Single protein structure of sequence from Sulfolobus solfataricus. Full crystallographic information is available from OCA.
Reference
The structural basis of substrate promiscuity in glucose dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus., Milburn CC, Lamble HJ, Theodossis A, Bull SD, Hough DW, Danson MJ, Taylor GL, J Biol Chem. 2006 May 26;281(21):14796-804. Epub 2006 Mar 23. PMID:16556607
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