1nwg
From Proteopedia
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[[Image:1nwg.gif|left|200px]] | [[Image:1nwg.gif|left|200px]] | ||
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'''BETA-1,4-GALACTOSYLTRANSFERASE COMPLEX WITH ALPHA-LACTALBUMIN AND N-BUTANOYL-GLUCOAMINE''' | '''BETA-1,4-GALACTOSYLTRANSFERASE COMPLEX WITH ALPHA-LACTALBUMIN AND N-BUTANOYL-GLUCOAMINE''' | ||
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==About this Structure== | ==About this Structure== | ||
- | 1NWG is a [[Protein complex]] structure of sequences 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 entry | + | 1NWG is a [[Protein complex]] structure of sequences 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 entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1jna 1jna]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NWG OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Ramakrishnan, B.]] | [[Category: Ramakrishnan, B.]] | ||
[[Category: Shah, P S.]] | [[Category: Shah, P S.]] | ||
- | [[Category: | + | [[Category: Alpha-lactalbumin]] |
- | [[Category: | + | [[Category: Beta1,4-galactosyltransferase]] |
- | [[Category: | + | [[Category: N-butanoyl-glucoamine]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:03:40 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 00:03, 3 May 2008
BETA-1,4-GALACTOSYLTRANSFERASE COMPLEX WITH ALPHA-LACTALBUMIN AND N-BUTANOYL-GLUCOAMINE
Overview
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.
About this Structure
1NWG is a Protein complex structure of sequences from Bos taurus and Mus musculus. This structure supersedes the now removed PDB entry 1jna. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Sat May 3 03:03:40 2008