1h7q

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[[Image:1h7q.jpg|left|200px]]
[[Image:1h7q.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1h7q |SIZE=350|CAPTION= <scene name='initialview01'>1h7q</scene>, resolution 2.00&Aring;
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The line below this paragraph, containing "STRUCTURE_1h7q", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Residue+A1259'>AC1</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=TYD:THYMIDINE-5&#39;-+DIPHOSPHATE'>TYD</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1h7q| PDB=1h7q | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h7q OCA], [http://www.ebi.ac.uk/pdbsum/1h7q PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1h7q RCSB]</span>
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}}
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'''DTDP-MANGANESE COMPLEX OF SPSA FROM BACILLUS SUBTILIS'''
'''DTDP-MANGANESE COMPLEX OF SPSA FROM BACILLUS SUBTILIS'''
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[[Category: Davies, G J.]]
[[Category: Davies, G J.]]
[[Category: Tarbouriech, N.]]
[[Category: Tarbouriech, N.]]
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[[Category: glycosyltransferase]]
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[[Category: Glycosyltransferase]]
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[[Category: transferase]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:32:30 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:59:37 2008''
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Revision as of 15:32, 2 May 2008

Image:1h7q.jpg

Template:STRUCTURE 1h7q

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. 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 Page seeded by OCA on Fri May 2 18:32:30 2008

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