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1x9d

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[[Image:1x9d.gif|left|200px]]
[[Image:1x9d.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1x9d |SIZE=350|CAPTION= <scene name='initialview01'>1x9d</scene>, resolution 1.410&Aring;
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The line below this paragraph, containing "STRUCTURE_1x9d", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=BU1:1,4-BUTANEDIOL'>BU1</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SMD:METHYL-2-S-(ALPHA-D-MANNOPYRANOSYL)-2-THIO-ALPHA-D-MANNOPYRANOSIDE'>SMD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Mannosyl-oligosaccharide_1,2-alpha-mannosidase Mannosyl-oligosaccharide 1,2-alpha-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.113 3.2.1.113] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= MAN1B1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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-->
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|DOMAIN=
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{{STRUCTURE_1x9d| PDB=1x9d | SCENE= }}
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|RELATEDENTRY=[[1fmi|1FMI]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1x9d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x9d OCA], [http://www.ebi.ac.uk/pdbsum/1x9d PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1x9d RCSB]</span>
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}}
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'''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'''
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[[Category: Tempel, W.]]
[[Category: Tempel, W.]]
[[Category: Wang, B C.]]
[[Category: Wang, B C.]]
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[[Category: glycosyl hydrolase]]
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[[Category: Glycosyl hydrolase]]
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[[Category: mannosidase]]
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[[Category: Mannosidase]]
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[[Category: substrate analogue]]
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[[Category: Substrate analogue]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:44:13 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:46:29 2008''
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Revision as of 11:44, 3 May 2008

Image:1x9d.gif


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


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.

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 Sat May 3 14:44:13 2008

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