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1o23

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Revision as of 09:01, 2 December 2020

CRYSTAL STRUCTURE OF LACTOSE SYNTHASE IN THE PRESENCE OF UDP-GLUCOSE

Structural highlights

1o23 is a 4 chain structure with sequence from Bovin and Lk3 transgenic mice. This structure supersedes the now removed PDB entries 1nt7 and 1jnc. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , , ,
Gene:	LALBA (LK3 transgenic mice), BETA1,4-GALACTOSYLTRANSFERASE (BOVIN)
Activity:	N-acetyllactosamine synthase, with EC number 2.4.1.90
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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. [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.

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

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.

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^[1]

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

References

↑ Ramakrishnan B, Shah PS, Qasba PK. 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. J Biol Chem. 2001 Oct 5;276(40):37665-71. Epub 2001 Aug 2. PMID:11485999 doi:10.1074/jbc.M102458200

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1o23"

@@ Line 1: / Line 1: @@
 ==CRYSTAL STRUCTURE OF LACTOSE SYNTHASE IN THE PRESENCE OF UDP-GLUCOSE==
-<StructureSection load='1o23' size='340' side='right' caption='[[1o23]], [[Resolution|resolution]] 2.32&Aring;' scene=''>
+<StructureSection load='1o23' size='340' side='right'caption='[[1o23]], [[Resolution|resolution]] 2.32&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1o23]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin] and [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1O23 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1o23]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin] and [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. 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 [http://proteopedia.org/fgij/fg.htm?mol=1O23 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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>
+</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>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LALBA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice]), BETA1,4-GALACTOSYLTRANSFERASE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </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=1o23 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o23 OCA], [http://pdbe.org/1o23 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o23 RCSB], [http://www.ebi.ac.uk/pdbsum/1o23 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1o23 ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1o23 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o23 OCA], [http://pdbe.org/1o23 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o23 RCSB], [http://www.ebi.ac.uk/pdbsum/1o23 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1o23 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 30: / Line 30: @@
 </div>
 <div class="pdbe-citations 1o23" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Alpha-lactalbumin 3D structures|Alpha-lactalbumin 3D structures]]
+*[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]]
 == References ==
 <references/>
@@ Line 35: / Line 39: @@
 </StructureSection>
 [[Category: Bovin]]
+[[Category: Large Structures]]
 [[Category: Lk3 transgenic mice]]
 [[Category: N-acetyllactosamine synthase]]

1o23

From Proteopedia

Revision as of 09:01, 2 December 2020

CRYSTAL STRUCTURE OF LACTOSE SYNTHASE IN THE PRESENCE OF UDP-GLUCOSE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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