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.

1fgx

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1fgx.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1fgx.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1fgx| PDB=1fgx | SCENE= }}
{{STRUCTURE_1fgx| PDB=1fgx | SCENE= }}
-
'''CRYSTAL STRUCTURE OF THE BOVINE BETA 1,4 GALACTOSYLTRANSFERASE (B4GALT1) CATALYTIC DOMAIN COMPLEXED WITH UMP'''
+
===CRYSTAL STRUCTURE OF THE BOVINE BETA 1,4 GALACTOSYLTRANSFERASE (B4GALT1) CATALYTIC DOMAIN COMPLEXED WITH UMP===
-
==Overview==
+
<!--
-
beta1,4-galactosyltransferase T1 (beta4Gal-T1, EC 2.4.1.90/38), a Golgi resident membrane-bound enzyme, transfers galactose from uridine diphosphogalactose to the terminal beta-N-acetylglucosamine residues forming the poly-N-acetyllactosamine core structures present in glycoproteins and glycosphingolipids. In mammals, beta4Gal-T1 binds to alpha-lactalbumin, a protein that is structurally homologous to lyzozyme, to produce lactose. beta4Gal-T1 is a member of a large family of homologous beta4galactosyltransferases that use different types of glycoproteins and glycolipids as substrates. Here we solved and refined the crystal structures of recombinant bovine beta4Gal-T1 to 2.4 A resolution in the presence and absence of the substrate uridine diphosphogalactose. The crystal structure of the bovine substrate-free beta4Gal-T1 catalytic domain showed a new fold consisting of a single conical domain with a large open pocket at its base. In the substrate-bound complex, the pocket encompassed residues interacting with uridine diphosphogalactose. The structure of the complex contained clear regions of electron density for the uridine diphosphate portion of the substrate, where its beta-phosphate group was stabilized by hydrogen-bonding contacts with conserved residues including the Asp252ValAsp254 motif. These results help the interpretation of engineered beta4Gal-T1 point mutations. They suggest a mechanism possibly involved in galactose transfer and enable identification of the critical amino acids involved in alpha-lactalbumin interactions.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10393171}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10393171 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10393171}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Alpha beta alpha fold]]
[[Category: Alpha beta alpha fold]]
[[Category: Nucleotide binding protein]]
[[Category: Nucleotide binding protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:18:48 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:13:54 2008''

Revision as of 00:13, 1 July 2008

Image:1fgx.png

Template:STRUCTURE 1fgx

CRYSTAL STRUCTURE OF THE BOVINE BETA 1,4 GALACTOSYLTRANSFERASE (B4GALT1) CATALYTIC DOMAIN COMPLEXED WITH UMP

Template:ABSTRACT PUBMED 10393171

About this Structure

1FGX is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

Crystal structures of the bovine beta4galactosyltransferase catalytic domain and its complex with uridine diphosphogalactose., Gastinel LN, Cambillau C, Bourne Y, EMBO J. 1999 Jul 1;18(13):3546-57. PMID:10393171

Page seeded by OCA on Tue Jul 1 03:13:54 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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