2jzc

From Proteopedia

(Difference between revisions)

Revision as of 11:18, 18 July 2018

NMR solution structure of ALG13: The sugar donor subunit of a yeast N-acetylglucosamine transferase. Northeast Structural Genomics Consortium target YG1

Structural highlights

2jzc is a 1 chain structure with sequence from Atcc 18824. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	ALG13, YGL047W (ATCC 18824)
Activity:	N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase, with EC number 2.4.1.141
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

[ALG13_YEAST] Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The solution structure of Alg13, the glycosyl donor-binding domain of an important bipartite glycosyltransferase in the yeast Saccharomyces cerevisiae, is presented. This glycosyltransferase is unusual in that it is active only in the presence of a binding partner, Alg14. Alg13 is found to adopt a unique topology among glycosyltransferases. Rather than the conventional Rossmann fold found in all GT-B enzymes, the N-terminal half of the protein is a Rossmann-like fold with a mixed parallel and antiparallel beta sheet. The Rossmann fold of the C-terminal half of Alg13 is conserved. However, although conventional GT-B enzymes usually possess three helices at the C terminus, only two helices are present in Alg13. Titration of Alg13 with both UDP-GlcNAc, the native glycosyl donor, and a paramagnetic mimic, UDP-TEMPO, shows that the interaction of Alg13 with the sugar donor is primarily through the residues in the C-terminal half of the protein.

Solution structure of Alg13: the sugar donor subunit of a yeast N-acetylglucosamine transferase.,Wang X, Weldeghiorghis T, Zhang G, Imperiali B, Prestegard JH Structure. 2008 Jun;16(6):965-75. PMID:18547528^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Chantret I, Dancourt J, Barbat A, Moore SE. Two proteins homologous to the N- and C-terminal domains of the bacterial glycosyltransferase Murg are required for the second step of dolichyl-linked oligosaccharide synthesis in Saccharomyces cerevisiae. J Biol Chem. 2005 Mar 11;280(10):9236-42. Epub 2004 Dec 22. PMID:15615718 doi:http://dx.doi.org/M413941200
↑ Gao XD, Tachikawa H, Sato T, Jigami Y, Dean N. Alg14 recruits Alg13 to the cytoplasmic face of the endoplasmic reticulum to form a novel bipartite UDP-N-acetylglucosamine transferase required for the second step of N-linked glycosylation. J Biol Chem. 2005 Oct 28;280(43):36254-62. Epub 2005 Aug 12. PMID:16100110 doi:http://dx.doi.org/M507569200
↑ Wang X, Weldeghiorghis T, Zhang G, Imperiali B, Prestegard JH. Solution structure of Alg13: the sugar donor subunit of a yeast N-acetylglucosamine transferase. Structure. 2008 Jun;16(6):965-75. PMID:18547528 doi:10.1016/j.str.2008.03.010

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2jzc"

@@ Line 1: / Line 1: @@
 ==NMR solution structure of ALG13: The sugar donor subunit of a yeast N-acetylglucosamine transferase. Northeast Structural Genomics Consortium target YG1==
 <StructureSection load='2jzc' size='340' side='right' caption='[[2jzc]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ALG13, YGL047W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N-acetylglucosaminyldiphosphodolichol_N-acetylglucosaminyltransferase N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.141 2.4.1.141] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2jzc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jzc OCA], [http://pdbe.org/2jzc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jzc RCSB], [http://www.ebi.ac.uk/pdbsum/2jzc PDBsum], [http://www.topsan.org/Proteins/NESGC/2jzc TOPSAN]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2jzc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jzc OCA], [http://pdbe.org/2jzc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jzc RCSB], [http://www.ebi.ac.uk/pdbsum/2jzc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2jzc ProSAT], [http://www.topsan.org/Proteins/NESGC/2jzc TOPSAN]</span></td></tr>
 </table>
 == Function ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jz/2jzc_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jz/2jzc_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

2jzc

From Proteopedia

Revision as of 11:18, 18 July 2018

NMR solution structure of ALG13: The sugar donor subunit of a yeast N-acetylglucosamine transferase. Northeast Structural Genomics Consortium target YG1

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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