2nuy: Difference between revisions
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'''2-keto-3-deoxygluconate aldolase from Sulfolobus acidocaldarius in complex with pyruvate''' | {{Structure | ||
|PDB= 2nuy |SIZE=350|CAPTION= <scene name='initialview01'>2nuy</scene>, resolution 2.500Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=PYR:PYRUVIC ACID'>PYR</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/2-dehydro-3-deoxy-phosphogluconate_aldolase 2-dehydro-3-deoxy-phosphogluconate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.14 4.1.2.14] | |||
|GENE= saci_0225 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2285 Sulfolobus acidocaldarius]) | |||
}} | |||
'''2-keto-3-deoxygluconate aldolase from Sulfolobus acidocaldarius in complex with pyruvate''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2NUY is a [ | 2NUY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_acidocaldarius Sulfolobus acidocaldarius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NUY OCA]. | ||
==Reference== | ==Reference== | ||
Biochemical and structural exploration of the catalytic capacity of Sulfolobus KDG aldolases., Wolterink-van Loo S, van Eerde A, Siemerink MA, Akerboom J, Dijkstra BW, van der Oost J, Biochem J. 2007 May 1;403(3):421-30. PMID:[http:// | Biochemical and structural exploration of the catalytic capacity of Sulfolobus KDG aldolases., Wolterink-van Loo S, van Eerde A, Siemerink MA, Akerboom J, Dijkstra BW, van der Oost J, Biochem J. 2007 May 1;403(3):421-30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17176250 17176250] | ||
[[Category: 2-dehydro-3-deoxy-phosphogluconate aldolase]] | [[Category: 2-dehydro-3-deoxy-phosphogluconate aldolase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: tim barrel]] | [[Category: tim barrel]] | ||
''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 17:51:27 2008'' | ||
Revision as of 18:51, 20 March 2008
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| , resolution 2.500Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | saci_0225 (Sulfolobus acidocaldarius) | ||||||
| Activity: | 2-dehydro-3-deoxy-phosphogluconate aldolase, with EC number 4.1.2.14 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
2-keto-3-deoxygluconate aldolase from Sulfolobus acidocaldarius in complex with pyruvate
OverviewOverview
Aldolases are enzymes with potential applications in biosynthesis, depending on their activity, specificity and stability. In the present study, the genomes of Sulfolobus species were screened for aldolases. Two new KDGA [2-keto-3-deoxygluconate (2-oxo-3-deoxygluconate) aldolases] from Sulfolobus acidocaldarius and Sulfolobus tokodaii were identified, overexpressed in Escherichia coli and characterized. Both enzymes were found to have biochemical properties similar to the previously characterized S. solfataricus KDGA, including the condensation of pyruvate and either D,L-glyceraldehyde or D,L-glyceraldehyde 3-phosphate. The crystal structure of S. acidocaldarius KDGA revealed the presence of a novel phosphate-binding motif that allows the formation of multiple hydrogen-bonding interactions with the acceptor substrate, and enables high activity with glyceraldehyde 3-phosphate. Activity analyses with unnatural substrates revealed that these three KDGAs readily accept aldehydes with two to four carbon atoms, and that even aldoses with five carbon atoms are accepted to some extent. Water-mediated interactions permit binding of substrates in multiple conformations in the spacious hydrophilic binding site, and correlate with the observed broad substrate specificity.
About this StructureAbout this Structure
2NUY is a Single protein structure of sequence from Sulfolobus acidocaldarius. Full crystallographic information is available from OCA.
ReferenceReference
Biochemical and structural exploration of the catalytic capacity of Sulfolobus KDG aldolases., Wolterink-van Loo S, van Eerde A, Siemerink MA, Akerboom J, Dijkstra BW, van der Oost J, Biochem J. 2007 May 1;403(3):421-30. PMID:17176250
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