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.


1orr

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1orr.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1orr.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1orr| PDB=1orr | SCENE= }}
{{STRUCTURE_1orr| PDB=1orr | SCENE= }}
-
'''Crystal Structure of CDP-Tyvelose 2-Epimerase complexed with NAD and CDP'''
+
===Crystal Structure of CDP-Tyvelose 2-Epimerase complexed with NAD and CDP===
-
==Overview==
+
<!--
-
Tyvelose epimerase catalyzes the last step in the biosynthesis of tyvelose by converting CDP-d-paratose to CDP-d-tyvelose. This unusual 3,6-dideoxyhexose occurs in the O-antigens of some types of Gram-negative bacteria. Here we describe the cloning, protein purification, and high-resolution x-ray crystallographic analysis of tyvelose epimerase from Salmonella typhi complexed with CDP. The enzyme from S. typhi is a homotetramer with each subunit containing 339 amino acid residues and a tightly bound NAD+ cofactor. The quaternary structure of the enzyme displays 222 symmetry and can be aptly described as a dimer of dimers. Each subunit folds into two distinct lobes: the N-terminal motif responsible for NAD+ binding and the C-terminal region that harbors the binding site for CDP. The analysis described here demonstrates that tyvelose epimerase belongs to the short-chain dehydrogenase/reductase superfamily of enzymes. Indeed, its active site is reminiscent to that observed for UDP-galactose 4-epimerase, an enzyme that plays a key role in galactose metabolism. Unlike UDP-galactose 4-epimerase where the conversion of configuration occurs about C-4 of the UDP-glucose or UDP-galactose substrates, in the reaction catalyzed by tyvelose epimerase, the inversion of stereochemistry occurs at C-2. On the basis of the observed binding mode for CDP, it is possible to predict the manner in which the substrate, CDP-paratose, and the product, CDP-tyvelose, might be accommodated within the active site of tyvelose epimerase.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12642575}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12642575 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12642575}}
==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 04:12:13 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 18:36:58 2008''

Revision as of 15:36, 28 July 2008

Image:1orr.png

Template:STRUCTURE 1orr

Crystal Structure of CDP-Tyvelose 2-Epimerase complexed with NAD and CDP

Template:ABSTRACT PUBMED 12642575

About this Structure

1ORR is a Single protein structure of sequence from Salmonella typhi. Full crystallographic information is available from OCA.

Reference

High resolution x-ray structure of tyvelose epimerase from Salmonella typhi., Koropatkin NM, Liu HW, Holden HM, J Biol Chem. 2003 Jun 6;278(23):20874-81. Epub 2003 Mar 17. PMID:12642575

Page seeded by OCA on Mon Jul 28 18:36:58 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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