1o0r

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(New page: 200px<br /><applet load="1o0r" size="450" color="white" frame="true" align="right" spinBox="true" caption="1o0r, resolution 2.30&Aring;" /> '''Crystal structure of...)
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[[Image:1o0r.jpg|left|200px]]<br /><applet load="1o0r" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1o0r, resolution 2.30&Aring;" />
 
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'''Crystal structure of the catalytic domain of bovine beta1,4-galactosyltransferase complex with UDP-galactose'''<br />
 
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==Overview==
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==Crystal structure of the catalytic domain of bovine beta1,4-galactosyltransferase complex with UDP-galactose==
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The crystal structure of the catalytic domain of bovine, beta1,4-galactosyltransferase (Gal-T1) co-crystallized with UDP-Gal and, MnCl(2) has been solved at 2.8 A resolution. The structure not only, identifies galactose, the donor sugar binding site in Gal-T1, but also, reveals an oligosaccharide acceptor binding site. The galactose moiety of, UDP-Gal is found deep inside the catalytic pocket, interacting with, Asp252, Gly292, Gly315, Glu317 and Asp318 residues. Compared to the native, crystal structure reported earlier, the present UDP-Gal bound structure, exhibits a large conformational change in residues 345-365 and a change in, the side-chain orientation of Trp314. Thus, the binding of UDP-Gal induces, a conformational change in Gal-T1, which not only creates the acceptor, binding pocket for N-acetylglucosamine (GlcNAc) but also establishes the, binding site for an extended sugar acceptor. The presence of a binding, site that accommodates an extended sugar offers an explanation for the, observation that an oligosaccharide with GlcNAc at the non-reducing end, serves as a better acceptor than the monosaccharide, GlcNAc. Modeling, studies using oligosaccharide acceptors indicate that a pentasaccharide, such as N-glycans with GlcNAc at their non-reducing ends, fits the site, best. A sequence comparison of the human Gal-T family members indicates, that although the binding site for the GlcNAc residue is highly conserved, the site that binds the extended sugar exhibits large variations. This is, an indication that different Gal-T family members prefer different types, of glycan acceptors with GlcNAc at their non-reducing ends.
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<StructureSection load='1o0r' size='340' side='right'caption='[[1o0r]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1o0r]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1kyb 1kyb]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O0R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O0R FirstGlance]. <br>
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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]] 2.3&#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=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=GDU:GALACTOSE-URIDINE-5-DIPHOSPHATE'>GDU</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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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=1o0r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o0r OCA], [https://pdbe.org/1o0r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o0r RCSB], [https://www.ebi.ac.uk/pdbsum/1o0r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o0r ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/B4GT1_BOVIN B4GT1_BOVIN] The Golgi complex form catalyzes the production of lactose in the lactating mammary gland and could also be responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. The cell surface form functions as a recognition molecule during a variety of cell to cell and cell to matrix interactions, as those occurring during development and egg fertilization, by binding to specific oligosaccharide ligands on opposing cells or in the extracellular matrix.
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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/o0/1o0r_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=1o0r ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1O0R is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with GDU, MN, SO4, MES and DIO as [http://en.wikipedia.org/wiki/ligands ligands]. This structure superseeds the now removed PDB entry 1KYB. Active as [http://en.wikipedia.org/wiki/N-acetyllactosamine_synthase N-acetyllactosamine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.90 2.4.1.90] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1O0R OCA].
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*[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structure of beta1,4-galactosyltransferase complex with UDP-Gal reveals an oligosaccharide acceptor binding site., Ramakrishnan B, Balaji PV, Qasba PK, J Mol Biol. 2002 Apr 26;318(2):491-502. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12051854 12051854]
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: N-acetyllactosamine synthase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Balaji PV]]
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[[Category: Balaji, P.V.]]
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[[Category: Qasba PK]]
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[[Category: Qasba, P.K.]]
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[[Category: Ramakrishnan B]]
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[[Category: Ramakrishnan, B.]]
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[[Category: DIO]]
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[[Category: GDU]]
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[[Category: MES]]
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[[Category: MN]]
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[[Category: SO4]]
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[[Category: 4-galactosyltransferase]]
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[[Category: beta1]]
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[[Category: conformation ii]]
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[[Category: udp-gal]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:42:51 2007''
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Current revision

Crystal structure of the catalytic domain of bovine beta1,4-galactosyltransferase complex with UDP-galactose

PDB ID 1o0r

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