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.


2ftw

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2ftw.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2ftw.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2ftw| PDB=2ftw | SCENE= }}
{{STRUCTURE_2ftw| PDB=2ftw | SCENE= }}
-
'''Crystal structure of dihydropyrimidinase from dictyostelium discoideum'''
+
===Crystal structure of dihydropyrimidinase from dictyostelium discoideum===
-
==Overview==
+
<!--
-
In eukaryotes, dihydropyrimidinase catalyzes the second step of the reductive pyrimidine degradation, the reversible hydrolytic ring opening of dihydropyrimidines. Here we describe the three-dimensional structures of dihydropyrimidinase from two eukaryotes, the yeast Saccharomyces kluyveri and the slime mold Dictyostelium discoideum, determined and refined to 2.4 and 2.05 angstroms, respectively. Both enzymes have a (beta/alpha)8-barrel structural core embedding the catalytic di-zinc center, which is accompanied by a smaller beta-sandwich domain. Despite loop-forming insertions in the sequence of the yeast enzyme, the overall structures and architectures of the active sites of the dihydropyrimidinases are strikingly similar to each other, as well as to those of hydantoinases, dihydroorotases, and other members of the amidohydrolase superfamily of enzymes. However, formation of the physiologically relevant tetramer shows subtle but nonetheless significant differences. The extension of one of the sheets of the beta-sandwich domain across a subunit-subunit interface in yeast dihydropyrimidinase underlines its closer evolutionary relationship to hydantoinases, whereas the slime mold enzyme shows higher similarity to the noncatalytic collapsin-response mediator proteins involved in neuron development. Catalysis is expected to follow a dihydroorotase-like mechanism but in the opposite direction and with a different substrate. Complexes with dihydrouracil and N-carbamyl-beta-alanine obtained for the yeast dihydropyrimidinase reveal the mode of substrate and product binding and allow conclusions about what determines substrate specificity, stereoselectivity, and the reaction direction among cyclic amidohydrolases.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16517602}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16517602 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16517602}}
==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Lohkamp, B.]]
[[Category: Lohkamp, B.]]
[[Category: Beta-sandwich]]
[[Category: Beta-sandwich]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:18:12 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:02:40 2008''

Revision as of 11:02, 27 July 2008

Image:2ftw.png

Template:STRUCTURE 2ftw

Crystal structure of dihydropyrimidinase from dictyostelium discoideum

Template:ABSTRACT PUBMED 16517602

About this Structure

2FTW is a Single protein structure of sequence from Dictyostelium discoideum. Full crystallographic information is available from OCA.

Reference

The crystal structures of dihydropyrimidinases reaffirm the close relationship between cyclic amidohydrolases and explain their substrate specificity., Lohkamp B, Andersen B, Piskur J, Dobritzsch D, J Biol Chem. 2006 May 12;281(19):13762-76. Epub 2006 Mar 3. PMID:16517602

Page seeded by OCA on Sun Jul 27 14:02:40 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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