1ga8

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(New page: 200px<br /><applet load="1ga8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ga8, resolution 2.00&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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'''CRYSTAL STRUCTURE OF GALACOSYLTRANSFERASE LGTC IN COMPLEX WITH DONOR AND ACCEPTOR SUGAR ANALOGS.'''<br />
'''CRYSTAL STRUCTURE OF GALACOSYLTRANSFERASE LGTC IN COMPLEX WITH DONOR AND ACCEPTOR SUGAR ANALOGS.'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1GA8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis] with DEL, MN and UPF as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GA8 OCA].
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1GA8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis] with <scene name='pdbligand=DEL:'>DEL</scene>, <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=UPF:'>UPF</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GA8 OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Diekelmann, M.]]
[[Category: Diekelmann, M.]]
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[[Category: Ly, H.D.]]
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[[Category: Ly, H D.]]
[[Category: Persson, K.]]
[[Category: Persson, K.]]
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[[Category: Strynadka, N.C.J.]]
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[[Category: Strynadka, N C.J.]]
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[[Category: Wakarchuk, W.W.]]
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[[Category: Wakarchuk, W W.]]
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[[Category: Withers, S.G.]]
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[[Category: Withers, S G.]]
[[Category: DEL]]
[[Category: DEL]]
[[Category: MN]]
[[Category: MN]]
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[[Category: alpha-beta protein]]
[[Category: alpha-beta protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 01:05:46 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:47:56 2008''

Revision as of 10:48, 21 February 2008


1ga8, resolution 2.00Å

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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 with , and as ligands. Active as Lipopolysaccharide 3-alpha-galactosyltransferase, with EC number 2.4.1.44 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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