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.


2a6x

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2a6x.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2a6x.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2a6x| PDB=2a6x | SCENE= }}
{{STRUCTURE_2a6x| PDB=2a6x | SCENE= }}
-
'''Crystal structure of Emp46p carbohydrate recognition domain (CRD), Y131F mutant'''
+
===Crystal structure of Emp46p carbohydrate recognition domain (CRD), Y131F mutant===
-
==Overview==
+
<!--
-
Emp46p and Emp47p are type I membrane proteins, which cycle between the endoplasmic reticulum (ER) and the Golgi apparatus by vesicles coated with coat protein complexes I and II (COPI and COPII). They are considered to function as cargo receptors for exporting N-linked glycoproteins from the ER. We have determined crystal structures of the carbohydrate recognition domains (CRDs) of Emp46p and Emp47p of Saccharomyces cerevisiae, in the absence and presence of metal ions. Both proteins fold as a beta-sandwich, and resemble that of the mammalian ortholog, p58/ERGIC-53. However, the nature of metal binding is distinct from that of Ca(2+)-dependent p58/ERGIC-53. Interestingly, the CRD of Emp46p does not bind Ca(2+) ion but instead binds K(+) ion at the edge of a concave beta-sheet whose position is distinct from the corresponding site of the Ca(2+) ion in p58/ERGIC-53. Binding of K(+) ion to Emp46p appears essential for transport of a subset of glycoproteins because the Y131F mutant of Emp46p, which cannot bind K(+) ion fails to rescue the transport in disruptants of EMP46 and EMP47 genes. In contrast the CRD of Emp47p binds no metal ions at all. Furthermore, the CRD of Emp46p binds to glycoproteins carrying high mannosetype glycans and the is promoted by binding not the addition of Ca(2+) or K(+) ion in These results suggest that Emp46p can be regarded as a Ca(2+)-independent intracellular lectin at the ER exit sites.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16439369}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16439369 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16439369}}
==About this Structure==
==About this Structure==
Line 38: Line 42:
[[Category: Rsgi]]
[[Category: Rsgi]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:41:02 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:26:18 2008''

Revision as of 00:26, 28 July 2008

Image:2a6x.png

Template:STRUCTURE 2a6x

Crystal structure of Emp46p carbohydrate recognition domain (CRD), Y131F mutant

Template:ABSTRACT PUBMED 16439369

About this Structure

2A6X is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Structures of the carbohydrate recognition domain of Ca2+-independent cargo receptors Emp46p and Emp47p., Satoh T, Sato K, Kanoh A, Yamashita K, Yamada Y, Igarashi N, Kato R, Nakano A, Wakatsuki S, J Biol Chem. 2006 Apr 14;281(15):10410-9. Epub 2006 Jan 26. PMID:16439369

Page seeded by OCA on Mon Jul 28 03:26:18 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2a6x"
Personal tools