1ga8

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|PDB= 1ga8 |SIZE=350|CAPTION= <scene name='initialview01'>1ga8</scene>, resolution 2.00&Aring;
|PDB= 1ga8 |SIZE=350|CAPTION= <scene name='initialview01'>1ga8</scene>, resolution 2.00&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=DEL:4-DEOXYLACTOSE'>DEL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> and <scene name='pdbligand=UPF:URIDINE-5&#39;-DIPHOSPHATE-2-DEOXY-2-FLUOROGALACTOSE'>UPF</scene>
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|LIGAND= <scene name='pdbligand=DEL:4-DEOXYLACTOSE'>DEL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=UPF:URIDINE-5&#39;-DIPHOSPHATE-2-DEOXY-2-FLUOROGALACTOSE'>UPF</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Lipopolysaccharide_3-alpha-galactosyltransferase Lipopolysaccharide 3-alpha-galactosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.44 2.4.1.44]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Lipopolysaccharide_3-alpha-galactosyltransferase Lipopolysaccharide 3-alpha-galactosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.44 2.4.1.44] </span>
|GENE= LGTC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=487 Neisseria meningitidis])
|GENE= LGTC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=487 Neisseria meningitidis])
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|DOMAIN=
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|RELATEDENTRY=[[1g9r|1G9R]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ga8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ga8 OCA], [http://www.ebi.ac.uk/pdbsum/1ga8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ga8 RCSB]</span>
}}
}}
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[[Category: Wakarchuk, W W.]]
[[Category: Wakarchuk, W W.]]
[[Category: Withers, S G.]]
[[Category: Withers, S G.]]
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[[Category: DEL]]
 
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[[Category: MN]]
 
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[[Category: UPF]]
 
[[Category: alpha-beta protein]]
[[Category: alpha-beta protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 11:54:27 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:39:57 2008''

Revision as of 17:39, 30 March 2008


PDB ID 1ga8

Drag the structure with the mouse to rotate
, resolution 2.00Å
Ligands: , , ,
Gene: LGTC (Neisseria meningitidis)
Activity: Lipopolysaccharide 3-alpha-galactosyltransferase, with EC number 2.4.1.44
Related: 1G9R


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF GALACOSYLTRANSFERASE LGTC IN COMPLEX WITH DONOR AND ACCEPTOR SUGAR ANALOGS.


Overview

Many bacterial pathogens express lipooligosaccharides that mimic human cell surface glycoconjugates, enabling them to attach to host receptors and to evade the immune response. In Neisseria meningitidis, the galactosyltransferase LgtC catalyzes a key step in the biosynthesis of lipooligosaccharide structure by transferring alpha-d-galactose from UDP-galactose to a terminal lactose. The product retains the configuration of the donor sugar glycosidic bond; LgtC is thus a retaining glycosyltranferase. We report the 2 A crystal structures of the complex of LgtC with manganese and UDP 2-deoxy-2-fluoro-galactose (a donor sugar analog) in the presence and absence of the acceptor sugar analog 4'-deoxylactose. The structures, together with results from site-directed mutagenesis and kinetic analysis, give valuable insights into the unique catalytic mechanism and, as the first structure of a glycosyltransferase in complex with both the donor and acceptor sugars, provide a starting point for inhibitor design.

About this Structure

1GA8 is a Single protein structure of sequence from Neisseria meningitidis. Full crystallographic information is available from OCA.

Reference

Crystal structure of the retaining galactosyltransferase LgtC from Neisseria meningitidis in complex with donor and acceptor sugar analogs., Persson K, Ly HD, Dieckelmann M, Wakarchuk WW, Withers SG, Strynadka NC, Nat Struct Biol. 2001 Feb;8(2):166-75. PMID:11175908

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