1h7l
From Proteopedia
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|PDB= 1h7l |SIZE=350|CAPTION= <scene name='initialview01'>1h7l</scene>, resolution 1.98Å | |PDB= 1h7l |SIZE=350|CAPTION= <scene name='initialview01'>1h7l</scene>, resolution 1.98Å | ||
|SITE= <scene name='pdbsite=TYD:Mg+Binding+Site+For+Residue+A1257'>TYD</scene> | |SITE= <scene name='pdbsite=TYD:Mg+Binding+Site+For+Residue+A1257'>TYD</scene> | ||
| - | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> | + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TYD:THYMIDINE-5'-+DIPHOSPHATE'>TYD</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h7l OCA], [http://www.ebi.ac.uk/pdbsum/1h7l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1h7l RCSB]</span> | ||
}} | }} | ||
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[[Category: Davies, G J.]] | [[Category: Davies, G J.]] | ||
[[Category: Tarbouriech, N.]] | [[Category: Tarbouriech, N.]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: TYD]] | ||
[[Category: glycosyltransferase]] | [[Category: glycosyltransferase]] | ||
[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:59:23 2008'' |
Revision as of 17:59, 30 March 2008
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| , resolution 1.98Å | |||||||
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| Sites: | |||||||
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
DTDP-MAGNESIUM 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
1H7L 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
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