1nxc

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1nxc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nxc, resolution 1.51&Aring;" /> '''Structure of mouse G...)
Current revision (08:40, 6 November 2024) (edit) (undo)
 
(19 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1nxc.jpg|left|200px]]<br /><applet load="1nxc" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1nxc, resolution 1.51&Aring;" />
 
-
'''Structure of mouse Golgi alpha-1,2-mannosidase IA reveals the molecular basis for substrate specificity among Class I enzymes (family 47 glycosidases)'''<br />
 
-
==Overview==
+
==Structure of mouse Golgi alpha-1,2-mannosidase IA reveals the molecular basis for substrate specificity among Class I enzymes (family 47 glycosidases)==
-
Three subfamilies of mammalian Class 1 processing alpha1,2-mannosidases, (family 47 glycosidases) play critical roles in the maturation of, Asn-linked glycoproteins in the endoplasmic reticulum (ER) and Golgi, complex as well as influencing the timing and recognition for disposal of, terminally unfolded proteins by ER-associated degradation. In an effort to, define the structural basis for substrate recognition among Class 1, mannosidases, we have crystallized murine Golgi mannosidase IA (space, group P2(1)2(1)2(1)), and the structure was solved to 1.5-A resolution by, molecular replacement. The enzyme assumes an (alphaalpha)(7) barrel, structure with a Ca(2+) ion coordinated at the base of the barrel similar, to other Class 1 mannosidases. Critical residues within the barrel, structure that coordinate the Ca(2+) ion or presumably bind and catalyze, the hydrolysis of the glycone are also highly conserved. A Man(6)GlcNAc(2), oligosaccharide attached to Asn(515) in the murine enzyme was found to, extend into the active site of an adjoining protein unit in the crystal, lattice in a presumed enzyme-product complex. In contrast to an analogous, complex previously isolated for Saccharomyces cerevisiae ER mannosidase I, the oligosaccharide in the active site of the murine Golgi enzyme assumes, a different conformation to present an alternate oligosaccharide branch, into the active site pocket. A comparison of the observed, protein-carbohydrate interactions for the murine Golgi enzyme with the, binding cleft topologies of the other family 47 glycosidases provides a, framework for understanding the structural basis for substrate recognition, among this class of enzymes.
+
<StructureSection load='1nxc' size='340' side='right'caption='[[1nxc]], [[Resolution|resolution]] 1.51&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1nxc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NXC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NXC FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.51&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
 +
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nxc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nxc OCA], [https://pdbe.org/1nxc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nxc RCSB], [https://www.ebi.ac.uk/pdbsum/1nxc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nxc ProSAT], [https://www.topsan.org/Proteins/SECSG/1nxc TOPSAN]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/MA1A1_MOUSE MA1A1_MOUSE] Involved in the maturation of Asn-linked oligosaccharides. Progressively trim alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2).
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nx/1nxc_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1nxc ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Three subfamilies of mammalian Class 1 processing alpha1,2-mannosidases (family 47 glycosidases) play critical roles in the maturation of Asn-linked glycoproteins in the endoplasmic reticulum (ER) and Golgi complex as well as influencing the timing and recognition for disposal of terminally unfolded proteins by ER-associated degradation. In an effort to define the structural basis for substrate recognition among Class 1 mannosidases, we have crystallized murine Golgi mannosidase IA (space group P2(1)2(1)2(1)), and the structure was solved to 1.5-A resolution by molecular replacement. The enzyme assumes an (alphaalpha)(7) barrel structure with a Ca(2+) ion coordinated at the base of the barrel similar to other Class 1 mannosidases. Critical residues within the barrel structure that coordinate the Ca(2+) ion or presumably bind and catalyze the hydrolysis of the glycone are also highly conserved. A Man(6)GlcNAc(2) oligosaccharide attached to Asn(515) in the murine enzyme was found to extend into the active site of an adjoining protein unit in the crystal lattice in a presumed enzyme-product complex. In contrast to an analogous complex previously isolated for Saccharomyces cerevisiae ER mannosidase I, the oligosaccharide in the active site of the murine Golgi enzyme assumes a different conformation to present an alternate oligosaccharide branch into the active site pocket. A comparison of the observed protein-carbohydrate interactions for the murine Golgi enzyme with the binding cleft topologies of the other family 47 glycosidases provides a framework for understanding the structural basis for substrate recognition among this class of enzymes.
-
==About this Structure==
+
Structure of mouse Golgi alpha-mannosidase IA reveals the molecular basis for substrate specificity among class 1 (family 47 glycosylhydrolase) alpha1,2-mannosidases.,Tempel W, Karaveg K, Liu ZJ, Rose J, Wang BC, Moremen KW J Biol Chem. 2004 Jul 9;279(28):29774-86. Epub 2004 Apr 21. PMID:15102839<ref>PMID:15102839</ref>
-
1NXC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with MAN and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NXC OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
Structure of mouse Golgi alpha-mannosidase IA reveals the molecular basis for substrate specificity among class 1 (family 47 glycosylhydrolase) alpha1,2-mannosidases., Tempel W, Karaveg K, Liu ZJ, Rose J, Wang BC, Moremen KW, J Biol Chem. 2004 Jul 9;279(28):29774-86. Epub 2004 Apr 21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15102839 15102839]
+
</div>
-
[[Category: Mannosyl-oligosaccharide 1,2-alpha-mannosidase]]
+
<div class="pdbe-citations 1nxc" style="background-color:#fffaf0;"></div>
-
[[Category: Mus musculus]]
+
-
[[Category: Single protein]]
+
-
[[Category: Karaveg, K.]]
+
-
[[Category: Liu, Z.J.]]
+
-
[[Category: Moremen, K.W.]]
+
-
[[Category: Rose, J.]]
+
-
[[Category: SECSG, Southeast.Collaboratory.for.Structural.Genomics.]]
+
-
[[Category: Tempel, W.]]
+
-
[[Category: Wang, B.C.]]
+
-
[[Category: CA]]
+
-
[[Category: MAN]]
+
-
[[Category: glycosidase]]
+
-
[[Category: mannosidase]]
+
-
[[Category: protein structure initiative]]
+
-
[[Category: psi]]
+
-
[[Category: secsg]]
+
-
[[Category: southeast collaboratory for structural genomics]]
+
-
[[Category: structural genomics]]
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:38:26 2007''
+
==See Also==
 +
*[[Mannosidase 3D structures|Mannosidase 3D structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
 +
[[Category: Mus musculus]]
 +
[[Category: Karaveg K]]
 +
[[Category: Liu Z-J]]
 +
[[Category: Moremen KW]]
 +
[[Category: Rose J]]
 +
[[Category: Tempel W]]
 +
[[Category: Wang B-C]]

Current revision

Structure of mouse Golgi alpha-1,2-mannosidase IA reveals the molecular basis for substrate specificity among Class I enzymes (family 47 glycosidases)

PDB ID 1nxc

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

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