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1nxc

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[[Image:1nxc.jpg|left|200px]]
 
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{{Structure
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==Structure of mouse Golgi alpha-1,2-mannosidase IA reveals the molecular basis for substrate specificity among Class I enzymes (family 47 glycosidases)==
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|PDB= 1nxc |SIZE=350|CAPTION= <scene name='initialview01'>1nxc</scene>, resolution 1.51&Aring;
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<StructureSection load='1nxc' size='340' side='right'caption='[[1nxc]], [[Resolution|resolution]] 1.51&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene> and <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
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<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>
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|ACTIVITY= [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]
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</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>
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|GENE= man1a ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
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<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>
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}}
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<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>
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</table>
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== Function ==
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[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).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nx/1nxc_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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'''Structure of mouse Golgi alpha-1,2-mannosidase IA reveals the molecular basis for substrate specificity among Class I enzymes (family 47 glycosidases)'''
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==See Also==
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*[[Mannosidase 3D structures|Mannosidase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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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.
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[[Category: Large Structures]]
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==About this Structure==
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1NXC is a [[Single protein]] structure of sequence from [http://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].
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==Reference==
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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://www.ncbi.nlm.nih.gov/pubmed/15102839 15102839]
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[[Category: Mannosyl-oligosaccharide 1,2-alpha-mannosidase]]
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Single protein]]
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[[Category: Karaveg K]]
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[[Category: Karaveg, K.]]
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[[Category: Liu Z-J]]
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[[Category: Liu, Z J.]]
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[[Category: Moremen KW]]
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[[Category: Moremen, K W.]]
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[[Category: Rose J]]
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[[Category: Rose, J.]]
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[[Category: Tempel W]]
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[[Category: SECSG, Southeast Collaboratory for Structural Genomics.]]
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[[Category: Wang B-C]]
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[[Category: Tempel, W.]]
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[[Category: Wang, B C.]]
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[[Category: CA]]
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[[Category: MAN]]
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[[Category: glycosidase]]
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[[Category: mannosidase]]
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[[Category: protein structure initiative]]
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[[Category: psi]]
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[[Category: secsg]]
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[[Category: southeast collaboratory for structural genomic]]
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[[Category: structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:02:55 2008''
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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

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