2nux
From Proteopedia
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|PDB= 2nux |SIZE=350|CAPTION= <scene name='initialview01'>2nux</scene>, resolution 2.500Å | |PDB= 2nux |SIZE=350|CAPTION= <scene name='initialview01'>2nux</scene>, resolution 2.500Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene> | + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= saci_0225 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2285 Sulfolobus acidocaldarius]) | |GENE= saci_0225 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2285 Sulfolobus acidocaldarius]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2nuw|2NUW]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2nux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nux OCA], [http://www.ebi.ac.uk/pdbsum/2nux PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2nux RCSB]</span> | ||
}} | }} | ||
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[[Category: Dijkstra, B W.]] | [[Category: Dijkstra, B W.]] | ||
[[Category: Eerde, A van.]] | [[Category: Eerde, A van.]] | ||
| - | [[Category: MG]] | ||
[[Category: tim barrel]] | [[Category: tim barrel]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:08:44 2008'' |
Revision as of 01:08, 31 March 2008
| |||||||
| , resolution 2.500Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | saci_0225 (Sulfolobus acidocaldarius) | ||||||
| Activity: | 2-dehydro-3-deoxy-phosphogluconate aldolase, with EC number 4.1.2.14 | ||||||
| Related: | 2NUW
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
2-keto-3-deoxygluconate aldolase from Sulfolobus acidocaldarius, native structure in p6522 at 2.5 A resolution
Overview
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 Structure
2NUX is a Single protein structure of sequence from Sulfolobus acidocaldarius. Full crystallographic information is available from OCA.
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:17176250
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