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1fr8

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Revision as of 11:00, 13 September 2017

CRYSTAL STRUCTURE OF THE BOVINE BETA 1,4 GALACTOSYLTRANSFERASE (B4GALT1) CATALYTIC DOMAIN COMPLEXED WITH URIDINE DIPHOSPHOGALACTOSE

Structural highlights

1fr8 is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1fgx
Activity:	Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase, with EC number 2.4.1.38
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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

beta1,4-galactosyltransferase T1 (beta4Gal-T1, EC 2.4.1.90/38), a Golgi resident membrane-bound enzyme, transfers galactose from uridine diphosphogalactose to the terminal beta-N-acetylglucosamine residues forming the poly-N-acetyllactosamine core structures present in glycoproteins and glycosphingolipids. In mammals, beta4Gal-T1 binds to alpha-lactalbumin, a protein that is structurally homologous to lyzozyme, to produce lactose. beta4Gal-T1 is a member of a large family of homologous beta4galactosyltransferases that use different types of glycoproteins and glycolipids as substrates. Here we solved and refined the crystal structures of recombinant bovine beta4Gal-T1 to 2.4 A resolution in the presence and absence of the substrate uridine diphosphogalactose. The crystal structure of the bovine substrate-free beta4Gal-T1 catalytic domain showed a new fold consisting of a single conical domain with a large open pocket at its base. In the substrate-bound complex, the pocket encompassed residues interacting with uridine diphosphogalactose. The structure of the complex contained clear regions of electron density for the uridine diphosphate portion of the substrate, where its beta-phosphate group was stabilized by hydrogen-bonding contacts with conserved residues including the Asp252ValAsp254 motif. These results help the interpretation of engineered beta4Gal-T1 point mutations. They suggest a mechanism possibly involved in galactose transfer and enable identification of the critical amino acids involved in alpha-lactalbumin interactions.

Crystal structures of the bovine beta4galactosyltransferase catalytic domain and its complex with uridine diphosphogalactose.,Gastinel LN, Cambillau C, Bourne Y EMBO J. 1999 Jul 1;18(13):3546-57. PMID:10393171^[1]

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

References

↑ Gastinel LN, Cambillau C, Bourne Y. Crystal structures of the bovine beta4galactosyltransferase catalytic domain and its complex with uridine diphosphogalactose. EMBO J. 1999 Jul 1;18(13):3546-57. PMID:10393171 doi:http://dx.doi.org/10.1093/emboj/18.13.3546

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/1fr8"

@@ Line 1: / Line 1: @@
 ==CRYSTAL STRUCTURE OF THE BOVINE BETA 1,4 GALACTOSYLTRANSFERASE (B4GALT1) CATALYTIC DOMAIN COMPLEXED WITH URIDINE DIPHOSPHOGALACTOSE==
 <StructureSection load='1fr8' size='340' side='right' caption='[[1fr8]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1fr8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FR8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FR8 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1fr8]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FR8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FR8 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDU:GALACTOSE-URIDINE-5-DIPHOSPHATE'>GDU</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fgx|1fgx]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-N-acetylglucosaminylglycopeptide_beta-1,4-galactosyltransferase Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.38 2.4.1.38] </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=1fr8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fr8 OCA], [http://pdbe.org/1fr8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fr8 RCSB], [http://www.ebi.ac.uk/pdbsum/1fr8 PDBsum]</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=1fr8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fr8 OCA], [http://pdbe.org/1fr8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fr8 RCSB], [http://www.ebi.ac.uk/pdbsum/1fr8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1fr8 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
     <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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=1fr8 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 37: / Line 38: @@
 </StructureSection>
 [[Category: Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase]]
-[[Category: Bovin]]
 [[Category: Bourne, Y]]
 [[Category: Cambillau, C]]

1fr8

From Proteopedia

Revision as of 11:00, 13 September 2017

CRYSTAL STRUCTURE OF THE BOVINE BETA 1,4 GALACTOSYLTRANSFERASE (B4GALT1) CATALYTIC DOMAIN COMPLEXED WITH URIDINE DIPHOSPHOGALACTOSE

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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