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.


1wvg

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1wvg.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1wvg.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1wvg| PDB=1wvg | SCENE= }}
{{STRUCTURE_1wvg| PDB=1wvg | SCENE= }}
-
'''Structure of CDP-D-glucose 4,6-dehydratase from Salmonella typhi'''
+
===Structure of CDP-D-glucose 4,6-dehydratase from Salmonella typhi===
-
==Overview==
+
<!--
-
Tyvelose is a unique 3,6-dideoxyhexose found in the O antigens of some pathogenic species of Yersinia and Salmonella. It is produced via a complex biochemical pathway that employs CDP-D-glucose as the starting ligand. CDP-D-glucose 4,6-dehydratase catalyzes the first irreversible step in the synthesis of this 3,6-dideoxysugar by converting CDP-D-glucose to CDP-4-keto-6-deoxyglucose via an NAD+ -dependent intramolecular oxidation-reduction reaction. Here, the cloning, protein purification and X-ray crystallographic analysis of CDP-D-glucose 4,6-dehydratase from Salmonella typhi complexed with the substrate analog CDP-D-xylose are described. Each subunit of the tetrameric enzyme folds into two domains. The N-terminal region contains a Rossmann fold and provides the platform for NAD(H) binding. The C-terminal motif is primarily composed of alpha-helices and houses the binding pocket for the CDP portion of the CDP-D-xylose ligand. The xylose moiety extends into the active-site cleft that is located between the two domains. Key residues involved in anchoring the sugar group to the protein include Ser134, Tyr159, Asn197 and Arg208. Strikingly, Ser134 O gamma and Tyr159 O eta sit within 2.9 A of the 4'-hydroxyl group of xylose. Additionally, the side chains of Asp135 and Lys136 are located at 3.5 and 3.2 A, respectively, from C-5 of xylose. In the structurally related dTDP-D-glucose 4,6-dehydratase, the Asp/Lys pair is replaced with an Asp/Glu couple. On the basis of this investigation, it can be speculated that Tyr159 serves as the catalytic base to abstract the 4'-hydroxyl proton from the sugar and that Asp135 and Lys136 play critical roles in the subsequent dehydration step that leads to the final product.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15805590}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15805590 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15805590}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Rossmann fold]]
[[Category: Rossmann fold]]
[[Category: Short-chain dehydrogenase/reductase]]
[[Category: Short-chain dehydrogenase/reductase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:11:32 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:45:35 2008''

Revision as of 10:45, 29 July 2008

Image:1wvg.png

Template:STRUCTURE 1wvg

Structure of CDP-D-glucose 4,6-dehydratase from Salmonella typhi

Template:ABSTRACT PUBMED 15805590

About this Structure

1WVG is a Single protein structure of sequence from Salmonella enterica subsp. enterica serovar typhi. Full crystallographic information is available from OCA.

Reference

Structure of CDP-D-glucose 4,6-dehydratase from Salmonella typhi complexed with CDP-D-xylose., Koropatkin NM, Holden HM, Acta Crystallogr D Biol Crystallogr. 2005 Apr;61(Pt 4):365-73. Epub 2005, Mar 24. PMID:15805590

Page seeded by OCA on Tue Jul 29 13:45:35 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1wvg"
Personal tools