View source for 3aag


==Crystal structure of C. jejuni pglb C-terminal domain==
<StructureSection load='3aag' size='340' side='right'caption='[[3aag]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3aag]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Camjr Camjr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AAG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AAG FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CJE1268, pglB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=195099 CAMJR])</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=3aag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aag OCA], [https://pdbe.org/3aag PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aag RCSB], [https://www.ebi.ac.uk/pdbsum/3aag PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aag ProSAT]</span></td></tr>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/PGLB_CAMJR PGLB_CAMJR]] Oligosaccharyltransferase that catalyzes the transfer of a preassembled heptasaccharide from a lipid donor to an asparagine residue in nascent polypeptide chains, affording a beta-linked glycan to the asparagine side chain of target proteins.<ref>PMID:20007322</ref>  
== 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/aa/3aag_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=3aag ConSurf].
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== Publication Abstract from PubMed ==
Oligosaccharyltransferase (OST) catalyzes the transfer of an oligosaccharide from a lipid donor to an asparagine residue in nascent polypeptide chains. In the bacterium Campylobacter jejuni, a single-subunit membrane protein, PglB, catalyzes N-glycosylation. We report the 2.8 A resolution crystal structure of the C-terminal globular domain of PglB and its comparison with the previously determined structure from the archaeon Pyrococcus AglB. The two distantly related oligosaccharyltransferases share unexpected structural similarity beyond that expected from the sequence comparison. The common architecture of the putative catalytic sites revealed a new catalytic motif in PglB. Site-directed mutagenesis analyses confirmed the contribution of this motif to the catalytic function. Bacterial PglB and archaeal AglB constitute a protein family of the catalytic subunit of OST along with STT3 from eukaryotes. A structure-aided multiple sequence alignment of the STT3/PglB/AglB protein family revealed three types of OST catalytic centers. This novel classification will provide a useful framework for understanding the enzymatic properties of the OST enzymes from Eukarya, Archaea, and Bacteria.

Comparative structural biology of eubacterial and archaeal oligosaccharyltransferases.,Maita N, Nyirenda J, Igura M, Kamishikiryo J, Kohda D J Biol Chem. 2010 Feb 12;285(7):4941-50. Epub 2009 Dec 9. PMID:20007322<ref>PMID:20007322</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3aag" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Camjr]]
[[Category: Large Structures]]
[[Category: Kohda, D]]
[[Category: Maita, N]]
[[Category: Multidomain]]
[[Category: Transferase]]