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1s4n

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Crystal structure of yeast alpha1,2-mannosyltransferase Kre2p/Mnt1p

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-[[Image:1s4n.gif|left|200px]]
- {{Structure
+==Crystal structure of yeast alpha1,2-mannosyltransferase Kre2p/Mnt1p==
-|PDB= 1s4n |SIZE=350|CAPTION= <scene name='initialview01'>1s4n</scene>, resolution 2.01&Aring;
+<StructureSection load='1s4n' size='340' side='right'caption='[[1s4n]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
+<table><tr><td colspan='2'>[[1s4n]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S4N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S4N FirstGlance]. <br>
-|ACTIVITY= [http://en.wikipedia.org/wiki/Glycolipid_2-alpha-mannosyltransferase Glycolipid 2-alpha-mannosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.131 2.4.1.131]
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.01&#8491;</td></tr>
-|GENE= KRE2, MNT1, YDR483W, D8035.26 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
+<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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</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=1s4n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s4n OCA], [https://pdbe.org/1s4n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s4n RCSB], [https://www.ebi.ac.uk/pdbsum/1s4n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s4n ProSAT]</span></td></tr>
+</table>
-'''Crystal structure of yeast alpha1,2-mannosyltransferase Kre2p/Mnt1p'''
+== Function ==
+[https://www.uniprot.org/uniprot/KRE2_YEAST KRE2_YEAST] Required for the attachment of the third mannose residue of O-linked saccharides.
+== Evolutionary Conservation ==
-==Overview==
+[[Image:Consurf_key_small.gif|200px|right]]
-Kre2p/Mnt1p is a Golgi alpha1,2-mannosyltransferase involved in the biosynthesis of Saccharomyces cerevisiae cell wall glycoproteins. The protein belongs to glycosyltransferase family 15, a member of which has been implicated in virulence of Candida albicans. We present the 2.0 A crystal structures of the catalytic domain of Kre2p/Mnt1p and its binary and ternary complexes with GDP/Mn(2+) and GDP/Mn(2+)/acceptor methyl-alpha-mannoside. The protein has a mixed alpha/beta fold similar to the glycosyltransferase-A (GT-A) fold. Although the GDP-mannose donor was used in the crystallization experiments and the GDP moiety is bound tightly to the active site, the mannose is not visible in the electron density. The manganese is coordinated by a modified DXD motif (EPD), with only the first glutamate involved in a direct interaction. The position of the donor mannose was modeled using the binary and ternary complexes of other GT-A enzymes. The C1" of the modeled donor mannose is within hydrogen-bonding distance of both the hydroxyl of Tyr(220) and the O2 of the acceptor mannose. The O2 of the acceptor mannose is also within hydrogen bond distance of the hydroxyl of Tyr(220). The structures, modeling, site-directed mutagenesis, and kinetic analysis suggest two possible catalytic mechanisms. Either a double-displacement mechanism with the hydroxyl of Tyr(220) as the potential nucleophile or alternatively, an S(N)i-like mechanism with Tyr(220) positioning the substrates for catalysis. The importance of Tyr(220) in both mechanisms is highlighted by a 3000-fold reduction in k(cat) in the Y220F mutant.
+Check<jmol>
+  <jmolCheckbox>
-==About this Structure==
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/s4/1s4n_consurf.spt"</scriptWhenChecked>
-S4N is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S4N OCA].
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
-==Reference==
+  </jmolCheckbox>
-Structure of Kre2p/Mnt1p: a yeast alpha1,2-mannosyltransferase involved in mannoprotein biosynthesis., Lobsanov YD, Romero PA, Sleno B, Yu B, Yip P, Herscovics A, Howell PL, J Biol Chem. 2004 Apr 23;279(17):17921-31. Epub 2004 Jan 28. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14752117 14752117]
+</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=1s4n ConSurf].
-[[Category: Glycolipid 2-alpha-mannosyltransferase]]
+<div style="clear:both"></div>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Saccharomyces cerevisiae]]
-[[Category: Single protein]]
+[[Category: Herscovics A]]
-[[Category: Herscovics, A.]]
+[[Category: Howell PL]]
-[[Category: Howell, P L.]]
+[[Category: Lobsanov YD]]
-[[Category: Lobsanov, Y D.]]
+[[Category: Romero PA]]
-[[Category: Romero, P A.]]
+[[Category: Sleno B]]
-[[Category: Sleno, B.]]
+[[Category: Yip P]]
-[[Category: Yip, P.]]
+[[Category: Yu B]]
-[[Category: Yu, B.]]
-[[Category: CL]]
-[[Category: GOL]]
-[[Category: alpha/beta fold]]
-[[Category: nucleotide-binding domain]]
-[[Category: rossmann fold]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:00:22 2008''

1s4n

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Crystal structure of yeast alpha1,2-mannosyltransferase Kre2p/Mnt1p

Structural highlights

Function

Evolutionary Conservation

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