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1qgq

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{{Seed}}
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{{STRUCTURE_1qgq| PDB=1qgq | SCENE= }}
{{STRUCTURE_1qgq| PDB=1qgq | SCENE= }}
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'''UDP-MANGANESE COMPLEX OF SPSA FROM BACILLUS SUBTILIS'''
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===UDP-MANGANESE COMPLEX OF SPSA FROM BACILLUS SUBTILIS===
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==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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(as it appears on PubMed at http://www.pubmed.gov), where 10350455 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10350455}}
==About this Structure==
==About this Structure==
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[[Category: Charnock, S J.]]
[[Category: Charnock, S J.]]
[[Category: Glycosyltransferase]]
[[Category: Glycosyltransferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:15:04 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:08:59 2008''

Revision as of 14:09, 27 July 2008

Image:1qgq.png

Template:STRUCTURE 1qgq

UDP-MANGANESE COMPLEX OF SPSA FROM BACILLUS SUBTILIS

Template:ABSTRACT PUBMED 10350455

About this Structure

1QGQ is a Single protein structure of sequence from Bacillus subtilis. 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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