1h7q

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[[Image:1h7q.jpg|left|200px]]<br /><applet load="1h7q" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1h7q.jpg|left|200px]]<br /><applet load="1h7q" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1h7q, resolution 2.00&Aring;" />
caption="1h7q, resolution 2.00&Aring;" />
'''DTDP-MANGANESE COMPLEX OF SPSA FROM BACILLUS SUBTILIS'''<br />
'''DTDP-MANGANESE COMPLEX OF SPSA FROM BACILLUS SUBTILIS'''<br />
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==About this Structure==
==About this Structure==
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1H7Q 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 MN, MG and TYD as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Mg Binding Site For Residue A1259'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H7Q OCA].
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1H7Q 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=MN:'>MN</scene>, <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=TYD:'>TYD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Mg+Binding+Site+For+Residue+A1259'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H7Q OCA].
==Reference==
==Reference==
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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 16:07:03 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:47:27 2008''

Revision as of 07:47, 3 February 2008


1h7q, resolution 2.00Å

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DTDP-MANGANESE COMPLEX OF SPSA FROM BACILLUS SUBTILIS

Overview

The vast majority of glycosidic-bond synthesis in nature is performed by, glycosyltransferases, which use activated glycosides as the sugar donor., Typically, the activated leaving group is a nucleoside phosphate, lipid, phosphate or phosphate. The nucleotide-sugar-dependent, glycosyltransferases fall into over 50 sequence-based families, with the, largest and most widespread family of inverting transferases named family, GT-2. Here, we present the three-dimensional crystal structure of SpsA, the first and currently the only structural representative from family, GT-2, in complex with both Mn-dTDP and Mg-dTDP at a resolution of 2 A., These structures reveal how SpsA and related enzymes may display, nucleotide plasticity and permit a comparison of the catalytic centre of, this enzyme with those from related sequence families whose, three-dimensional structures have recently been determined. Family GT-2, enzymes, together with enzymes from families 7, 13 and 43, appear to form, a clan of related structures with identical catalytic apparatus and, reaction mechanism.

About this Structure

1H7Q is a Single protein structure of sequence from Bacillus subtilis with , and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Three-dimensional structures of the Mn and Mg dTDP complexes of the family GT-2 glycosyltransferase SpsA: a comparison with related NDP-sugar glycosyltransferases., Tarbouriech N, Charnock SJ, Davies GJ, J Mol Biol. 2001 Dec 7;314(4):655-61. PMID:11733986

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