We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1s4o

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1s4o.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1s4o.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1s4o| PDB=1s4o | SCENE= }}
{{STRUCTURE_1s4o| PDB=1s4o | SCENE= }}
-
'''Crystal structure of yeast alpha1,2-mannosyltransferase Kre2p/Mnt1p: binary complex with GDP/Mn'''
+
===Crystal structure of yeast alpha1,2-mannosyltransferase Kre2p/Mnt1p: binary complex with GDP/Mn===
-
==Overview==
+
<!--
-
Kre2p/Mnt1p is a Golgi alpha1,2-mannosyltransferase involved in the biosynthesis of Saccharomyces cerevisiae cell wall glycoproteins. The protein belongs to glycosyltransferase family 15, a member of which has been implicated in virulence of Candida albicans. We present the 2.0 A crystal structures of the catalytic domain of Kre2p/Mnt1p and its binary and ternary complexes with GDP/Mn(2+) and GDP/Mn(2+)/acceptor methyl-alpha-mannoside. The protein has a mixed alpha/beta fold similar to the glycosyltransferase-A (GT-A) fold. Although the GDP-mannose donor was used in the crystallization experiments and the GDP moiety is bound tightly to the active site, the mannose is not visible in the electron density. The manganese is coordinated by a modified DXD motif (EPD), with only the first glutamate involved in a direct interaction. The position of the donor mannose was modeled using the binary and ternary complexes of other GT-A enzymes. The C1" of the modeled donor mannose is within hydrogen-bonding distance of both the hydroxyl of Tyr(220) and the O2 of the acceptor mannose. The O2 of the acceptor mannose is also within hydrogen bond distance of the hydroxyl of Tyr(220). The structures, modeling, site-directed mutagenesis, and kinetic analysis suggest two possible catalytic mechanisms. Either a double-displacement mechanism with the hydroxyl of Tyr(220) as the potential nucleophile or alternatively, an S(N)i-like mechanism with Tyr(220) positioning the substrates for catalysis. The importance of Tyr(220) in both mechanisms is highlighted by a 3000-fold reduction in k(cat) in the Y220F mutant.
+
The line below this paragraph, {{ABSTRACT_PUBMED_14752117}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 14752117 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_14752117}}
==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Nucleotide-binding domain]]
[[Category: Nucleotide-binding domain]]
[[Category: Rossmann fold]]
[[Category: Rossmann fold]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:17:34 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:38:11 2008''

Revision as of 02:38, 29 July 2008

Image:1s4o.png

Template:STRUCTURE 1s4o

Crystal structure of yeast alpha1,2-mannosyltransferase Kre2p/Mnt1p: binary complex with GDP/Mn

Template:ABSTRACT PUBMED 14752117

About this Structure

1S4O is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Structure of Kre2p/Mnt1p: a yeast alpha1,2-mannosyltransferase involved in mannoprotein biosynthesis., Lobsanov YD, Romero PA, Sleno B, Yu B, Yip P, Herscovics A, Howell PL, J Biol Chem. 2004 Apr 23;279(17):17921-31. Epub 2004 Jan 28. PMID:14752117

Page seeded by OCA on Tue Jul 29 05:38:11 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1s4o"
Personal tools