1o23: Difference between revisions

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-[[Image:1o23.png|left|200px]]
-<!--
+==CRYSTAL STRUCTURE OF LACTOSE SYNTHASE IN THE PRESENCE OF UDP-GLUCOSE==
-The line below this paragraph, containing "STRUCTURE_1o23", creates the "Structure Box" on the page.
+<StructureSection load='1o23' size='340' side='right'caption='[[1o23]], [[Resolution|resolution]] 2.32&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1o23]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1nt7 1nt7] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1jnc 1jnc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O23 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O23 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.32&#8491;</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>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene>, <scene name='pdbligand=UPG:URIDINE-5-DIPHOSPHATE-GLUCOSE'>UPG</scene></td></tr>
-{{STRUCTURE_1o23|  PDB=1o23  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1o23 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o23 OCA], [https://pdbe.org/1o23 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o23 RCSB], [https://www.ebi.ac.uk/pdbsum/1o23 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o23 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/LALBA_MOUSE LALBA_MOUSE] Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a good acceptor substrate for this enzyme. This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers galactose onto the N-acetylglucosamine of the oligosaccharide chains in glycoproteins.
+== 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/o2/1o23_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=1o23 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+beta-1,4-Galactosyltransferase 1 (Gal-T1) transfers galactose (Gal) from UDP-Gal to N-acetylglucosamine (GlcNAc), which constitutes its normal galactosyltransferase (Gal-T) activity. In the presence of alpha-lactalbumin (LA), it transfers Gal to Glc, which is its lactose synthase (LS) activity. It also transfers glucose (Glc) from UDP-Glc to GlcNAc, constituting the glucosyltransferase (Glc-T) activity, albeit at an efficiency of only 0.3-0.4% of Gal-T activity. In the present study, we show that LA increases this activity almost 30-fold. It also enhances the Glc-T activity toward various N-acyl substituted glucosamine acceptors. Steady state kinetic studies of Glc-T reaction show that the K(m) for the donor and acceptor substrates are high in the absence of LA. In the presence of LA, the K(m) for the acceptor substrate is reduced 30-fold, whereas for UDP-Glc it is reduced only 5-fold. In order to understand this property, we have determined the crystal structures of the Gal-T1.LA complex with UDP-Glc x Mn(2+) and with N-butanoyl-glucosamine (N-butanoyl-GlcN), a preferred sugar acceptor in the Glc-T activity. The crystal structures reveal that although the binding of UDP-Glc is quite similar to UDP-Gal, there are few significant differences observed in the hydrogen bonding interactions between UDP-Glc and Gal-T1. Based on the present kinetic and crystal structural studies, a possible explanation for the role of LA in the Glc-T activity has been proposed.
-===CRYSTAL STRUCTURE OF LACTOSE SYNTHASE IN THE PRESENCE OF UDP-GLUCOSE===
+alpha-Lactalbumin (LA) stimulates milk beta-1,4-galactosyltransferase I (beta 4Gal-T1) to transfer glucose from UDP-glucose to N-acetylglucosamine. Crystal structure of beta 4Gal-T1 x LA complex with UDP-Glc.,Ramakrishnan B, Shah PS, Qasba PK J Biol Chem. 2001 Oct 5;276(40):37665-71. Epub 2001 Aug 2. PMID:11485999<ref>PMID:11485999</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1o23" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_11485999}}, adds the Publication Abstract to the page
+*[[Alpha-lactalbumin 3D structures|Alpha-lactalbumin 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 11485999 is the PubMed ID number.
+*[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]]
--->
+== References ==
-{{ABSTRACT_PUBMED_11485999}}
+<references/>
+__TOC__
-==About this Structure==
+</StructureSection>
-[[1o23]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. This structure supersedes the now removed PDB entries  and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1jnc 1jnc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O23 OCA].
-==Reference==
-<ref group="xtra">PMID:011485999</ref><references group="xtra"/>
 [[Category: Bos taurus]]
+[[Category: Large Structures]]
 [[Category: Mus musculus]]
-[[Category: N-acetyllactosamine synthase]]
+[[Category: Qasba PK]]
-[[Category: Qasba, P K.]]
+[[Category: Ramakrishnan B]]
-[[Category: Ramakrishnan, B.]]
+[[Category: Shah PS]]
-[[Category: Shah, P S.]]
-[[Category: 4-galactosyltransferase]]
-[[Category: Alpha-lactalbumin]]
-[[Category: Beta]]
-[[Category: Transferase activator/transferase complex]]
-[[Category: Udp-glucose]]