This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2nux

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2nux.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2nux.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2nux| PDB=2nux | SCENE= }}
{{STRUCTURE_2nux| PDB=2nux | SCENE= }}
-
'''2-keto-3-deoxygluconate aldolase from Sulfolobus acidocaldarius, native structure in p6522 at 2.5 A resolution'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17176250}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17176250 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17176250}}
==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Eerde, A van.]]
[[Category: Eerde, A van.]]
[[Category: Tim barrel]]
[[Category: Tim barrel]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:56:18 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:56:44 2008''

Revision as of 05:56, 28 July 2008

Image:2nux.png

Template:STRUCTURE 2nux

2-keto-3-deoxygluconate aldolase from Sulfolobus acidocaldarius, native structure in p6522 at 2.5 A resolution

Template:ABSTRACT PUBMED 17176250

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

Page seeded by OCA on Mon Jul 28 08:56:44 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2nux"
Personal tools