1x9d

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1x9d.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1x9d.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1x9d| PDB=1x9d | SCENE= }}
{{STRUCTURE_1x9d| PDB=1x9d | SCENE= }}
-
'''Crystal Structure Of Human Class I alpha-1,2-Mannosidase In Complex With Thio-Disaccharide Substrate Analogue'''
+
===Crystal Structure Of Human Class I alpha-1,2-Mannosidase In Complex With Thio-Disaccharide Substrate Analogue===
-
==Overview==
+
<!--
-
Quality control in the endoplasmic reticulum (ER) determines the fate of newly synthesized glycoproteins toward either correct folding or disposal by ER-associated degradation. Initiation of the disposal process involves selective trimming of N-glycans attached to misfolded glycoproteins by ER alpha-mannosidase I and subsequent recognition by the ER degradation-enhancing alpha-mannosidase-like protein family of lectins, both members of glycosylhydrolase family 47. The unusual inverting hydrolytic mechanism catalyzed by members of this family is investigated here by a combination of kinetic and binding analyses of wild type and mutant forms of human ER alpha-mannosidase I as well as by structural analysis of a co-complex with an uncleaved thiodisaccharide substrate analog. These data reveal the roles of potential catalytic acid and base residues and the identification of a novel (3)S(1) sugar conformation for the bound substrate analog. The co-crystal structure described here, in combination with the (1)C(4) conformation of a previously identified co-complex with the glycone mimic, 1-deoxymannojirimycin, indicates that glycoside bond cleavage proceeds through a least motion conformational twist of a properly predisposed substrate in the -1 subsite. A novel (3)H(4) conformation is proposed as the exploded transition state.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15713668}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15713668 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15713668}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Mannosidase]]
[[Category: Mannosidase]]
[[Category: Substrate analogue]]
[[Category: Substrate analogue]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:44:13 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 16:23:50 2008''

Revision as of 13:23, 29 July 2008

Image:1x9d.png


PDB ID 1x9d

Drag the structure with the mouse to rotate
1x9d, resolution 1.41Å ()
Ligands: , , ,
Gene: MAN1B1 (Homo sapiens)
Activity: Mannosyl-oligosaccharide 1,2-alpha-mannosidase, with EC number 3.2.1.113
Related: 1fmi
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



Crystal Structure Of Human Class I alpha-1,2-Mannosidase In Complex With Thio-Disaccharide Substrate Analogue

Template:ABSTRACT PUBMED 15713668

About this Structure

1X9D is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Mechanism of class 1 (glycosylhydrolase family 47) {alpha}-mannosidases involved in N-glycan processing and endoplasmic reticulum quality control., Karaveg K, Siriwardena A, Tempel W, Liu ZJ, Glushka J, Wang BC, Moremen KW, J Biol Chem. 2005 Apr 22;280(16):16197-207. Epub 2005 Feb 15. PMID:15713668

Page seeded by OCA on Tue Jul 29 16:23:50 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1x9d"
Personal tools