3bfp

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[[Image:3bfp.jpg|left|200px]]<br /><applet load="3bfp" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="3bfp, resolution 1.750&Aring;" />
 
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'''Crystal Structure of apo-PglD from Campylobacter jejuni'''<br />
 
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==Overview==
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==Crystal Structure of apo-PglD from Campylobacter jejuni==
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Campylobacter jejuni is highly unusual among bacteria in forming N-linked, glycoproteins. The heptasaccharide produced by its pgl system is attached, to protein Asn through its terminal 2,4-diacetamido-2,4,6-trideoxy-d-Glc, (QuiNAc4NAc or N,N'-diacetylbacillosamine) moiety. The crucial, last part, of this sugar's synthesis is the acetylation of, UDP-2-acetamido-4-amino-2,4,6-trideoxy-d-Glc by the enzyme PglD, with, acetyl-CoA as a cosubstrate. We have determined the crystal structures of, PglD in CoA-bound and unbound forms, refined to 1.8 and 1.75 A resolution, respectively. PglD is a trimer of subunits each comprised of two domains, an N-terminal alpha/beta-domain and a C-terminal left-handed beta-helix., Few structural differences accompany CoA binding, except in the C-terminal, region following the beta-helix (residues 189-195), which adopts an, extended structure in the unbound form and folds to extend the beta-helix, upon binding CoA. Computational molecular docking suggests a different, mode of nucleotide-sugar binding with respect to the acetyl-CoA donor, with the molecules arranged in an "L-shape", compared with the "in-line", orientation in related enzymes. Modeling indicates that the oxyanion, intermediate would be stabilized by the NH group of Gly143', with His125', the most likely residue to function as a general base, removing H+ from, the amino group prior to nucleophilic attack at the carbonyl carbon of, acetyl-CoA. Site-specific mutations of active site residues confirmed the, importance of His125', Glu124', and Asn118. We conclude that Asn118 exerts, its function by stabilizing the intricate hydrogen bonding network within, the active site and that Glu124' may function to increase the pKa of the, putative general base, His125'.
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<StructureSection load='3bfp' size='340' side='right'caption='[[3bfp]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[3bfp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Campylobacter_jejuni Campylobacter jejuni]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BFP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BFP FirstGlance]. <br>
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3BFP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Campylobacter_jejuni Campylobacter jejuni] with <scene name='pdbligand=FLC:'>FLC</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Flc+Binding+Site+For+Residue+A+1'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BFP OCA].
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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]] 1.75&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene></td></tr>
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==Reference==
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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=3bfp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bfp OCA], [https://pdbe.org/3bfp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bfp RCSB], [https://www.ebi.ac.uk/pdbsum/3bfp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bfp ProSAT]</span></td></tr>
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Structure and Active Site Residues of PglD, an N-Acetyltransferase from the Bacillosamine Synthetic Pathway Required for N-Glycan Synthesis in Campylobacter jejuni(,)., Rangarajan ES, Ruane KM, Sulea T, Watson DC, Proteau A, Leclerc S, Cygler M, Matte A, Young NM, Biochemistry. 2008 Jan 17;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18198901 18198901]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PGLD_CAMJE PGLD_CAMJE] Acetyltransferase that modifies the UDP-4-amino-sugar to form UDP-N,N'-diacetylbacillosamine in the N-linked protein glycosylation pathway.<ref>PMID:17087520</ref> <ref>PMID:19448740</ref>
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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/bf/3bfp_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=3bfp ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Campylobacter jejuni]]
[[Category: Campylobacter jejuni]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: BSGI, Montreal-Kingston.Bacterial.Structural.Genomics.Initiative.]]
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[[Category: Cygler M]]
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[[Category: Cygler, M.]]
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[[Category: Leclerc S]]
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[[Category: Leclerc, S.]]
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[[Category: Matte A]]
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[[Category: Matte, A.]]
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[[Category: Proteau A]]
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[[Category: Proteau, A.]]
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[[Category: Rangarajan ES]]
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[[Category: Rangarajan, E.S.]]
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[[Category: Watson DC]]
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[[Category: Watson, D.C.]]
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[[Category: Young NM]]
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[[Category: Young, N.M.]]
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[[Category: FLC]]
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[[Category: bacillosamine]]
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[[Category: bsgi]]
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[[Category: coa binding protein]]
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[[Category: left-handed beta helix]]
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[[Category: mkbsgi]]
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[[Category: montreal-kingston bacterial structural genomics initiative]]
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[[Category: n-acetyltransferase]]
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[[Category: n-glycan biosynthesis]]
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[[Category: structural genomics]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 13 08:13:38 2008''
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Current revision

Crystal Structure of apo-PglD from Campylobacter jejuni

PDB ID 3bfp

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