1qgs

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(New page: 200px<br /><applet load="1qgs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qgs, resolution 2.0&Aring;" /> '''UDP-MAGNESIUM COMPLEX...)
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'''UDP-MAGNESIUM COMPLEX OF SPSA FROM BACILLUS SUBTILIS'''<br />
'''UDP-MAGNESIUM COMPLEX OF SPSA FROM BACILLUS SUBTILIS'''<br />
==Overview==
==Overview==
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The enzymatic formation of glycosidic bonds may be catalyzed by the, transfer of the glycosyl moiety from an activated, nucleotide-diphospho-sugar donor to a specific acceptor. SpsA is a, glycosyltransferase implicated in the synthesis of the spore coat of, Bacillus subtilis, whose homologues include cellulose synthase and many, lipopolysaccharide and bacterial O-antigen synthases. The, three-dimensional crystal structure of SpsA has been determined by, conventional MIR techniques at a resolution of 1.5 A. It is a two-domain, protein with a nucleotide-binding domain together with an acceptor binding, domain which features a disordered loop spanning the active site. The, structures of SpsA in complex with both Mg-UDP and Mn-UDP have also been, determined at 2.0 and 1.7 A, respectively. These complexes, together with, the sequence conservation, begin to shed light on the mechanism of this, ubiquitous family of inverting glycosyltransferases.
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The enzymatic formation of glycosidic bonds may be catalyzed by the transfer of the glycosyl moiety from an activated nucleotide-diphospho-sugar donor to a specific acceptor. SpsA is a glycosyltransferase implicated in the synthesis of the spore coat of Bacillus subtilis, whose homologues include cellulose synthase and many lipopolysaccharide and bacterial O-antigen synthases. The three-dimensional crystal structure of SpsA has been determined by conventional MIR techniques at a resolution of 1.5 A. It is a two-domain protein with a nucleotide-binding domain together with an acceptor binding domain which features a disordered loop spanning the active site. The structures of SpsA in complex with both Mg-UDP and Mn-UDP have also been determined at 2.0 and 1.7 A, respectively. These complexes, together with the sequence conservation, begin to shed light on the mechanism of this ubiquitous family of inverting glycosyltransferases.
==About this Structure==
==About this Structure==
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1QGS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with MG, UDP and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QGS OCA].
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1QGS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=UDP:'>UDP</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QGS OCA].
==Reference==
==Reference==
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[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Charnock, S.J.]]
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[[Category: Charnock, S J.]]
[[Category: GOL]]
[[Category: GOL]]
[[Category: MG]]
[[Category: MG]]
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[[Category: glycosyltransferase]]
[[Category: glycosyltransferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:40:41 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:39:22 2008''

Revision as of 12:39, 21 February 2008


1qgs, resolution 2.0Å

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UDP-MAGNESIUM COMPLEX OF SPSA FROM BACILLUS SUBTILIS

Overview

The enzymatic formation of glycosidic bonds may be catalyzed by the transfer of the glycosyl moiety from an activated nucleotide-diphospho-sugar donor to a specific acceptor. SpsA is a glycosyltransferase implicated in the synthesis of the spore coat of Bacillus subtilis, whose homologues include cellulose synthase and many lipopolysaccharide and bacterial O-antigen synthases. The three-dimensional crystal structure of SpsA has been determined by conventional MIR techniques at a resolution of 1.5 A. It is a two-domain protein with a nucleotide-binding domain together with an acceptor binding domain which features a disordered loop spanning the active site. The structures of SpsA in complex with both Mg-UDP and Mn-UDP have also been determined at 2.0 and 1.7 A, respectively. These complexes, together with the sequence conservation, begin to shed light on the mechanism of this ubiquitous family of inverting glycosyltransferases.

About this Structure

1QGS is a Single protein structure of sequence from Bacillus subtilis with , and as ligands. Full crystallographic information is available from OCA.

Reference

Structure of the nucleotide-diphospho-sugar transferase, SpsA from Bacillus subtilis, in native and nucleotide-complexed forms., Charnock SJ, Davies GJ, Biochemistry. 1999 May 18;38(20):6380-5. PMID:10350455

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