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.


2p56

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2p56.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2p56.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2p56| PDB=2p56 | SCENE= }}
{{STRUCTURE_2p56| PDB=2p56 | SCENE= }}
-
'''Crystal structure of alpha-2,3-sialyltransferase from Campylobacter jejuni in apo form'''
+
===Crystal structure of alpha-2,3-sialyltransferase from Campylobacter jejuni in apo form===
-
==Overview==
+
<!--
-
Sialic acid is an essential sugar in biology that plays key roles in numerous cellular processes and interactions. The biosynthesis of sialylated glycoconjugates is catalyzed by five distinct families of sialyltransferases. In the last 25 years, there has been much research on the enzymes themselves, their genes, and their reaction products, but we still do not know the precise molecular mechanism of action for this class of glycosyltransferase. We previously reported the first detailed structural and kinetic characterization of Cst-II, a bifunctional sialyltransferase (CAZy GT-42) from the bacterium Campylobacter jejuni [Chiu et al. (2004) Nat. Struct. Mol. Biol. 11, 163-170]. This enzyme can use both Gal-beta-1,3/4-R and Neu5Ac-alpha-2,3-Gal-beta-1,3/4-R as acceptor sugars. A second sialyltransferase from this bacterium, Cst-I, has been shown to utilize solely Gal-beta-1,3/4-R as the acceptor sugar in its transferase reaction. We report here the structural and kinetic characterization of this monofunctional enzyme, which belongs to the same sialyltransferase family as Cst-II, in both apo and substrate bound form. Our structural data show that Cst-I adopts a similar GTA-type glycosyltransferase fold to that of the bifunctional Cst-II, with conservation of several key noncharged catalytic residues. Significant differences are found, however, between the two enzymes in the lid domain region, which is critical to the creation of the acceptor sugar binding site. Furthermore, molecular modeling of various acceptor sugars within the active sites of these enzymes provides significant new insights into the structural basis for substrate specificities within this biologically important enzyme class.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17518445}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17518445 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17518445}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Withers, S G.]]
[[Category: Withers, S G.]]
[[Category: Mixed alpha beta]]
[[Category: Mixed alpha beta]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 12:23:12 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:03:15 2008''

Revision as of 16:03, 27 July 2008

Image:2p56.png

Template:STRUCTURE 2p56

Crystal structure of alpha-2,3-sialyltransferase from Campylobacter jejuni in apo form

Template:ABSTRACT PUBMED 17518445

About this Structure

2P56 is a Single protein structure of sequence from Campylobacter jejuni. Full crystallographic information is available from OCA.

Reference

Structural analysis of the alpha-2,3-sialyltransferase Cst-I from Campylobacter jejuni in apo and substrate-analogue bound forms., Chiu CP, Lairson LL, Gilbert M, Wakarchuk WW, Withers SG, Strynadka NC, Biochemistry. 2007 Jun 19;46(24):7196-204. Epub 2007 May 23. PMID:17518445

Page seeded by OCA on Sun Jul 27 19:03:15 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2p56"
Personal tools