1h7q
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1h7q |SIZE=350|CAPTION= <scene name='initialview01'>1h7q</scene>, resolution 2.00Å | |PDB= 1h7q |SIZE=350|CAPTION= <scene name='initialview01'>1h7q</scene>, resolution 2.00Å | ||
|SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Residue+A1259'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Residue+A1259'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=TYD:THYMIDINE-5 | + | |LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=TYD:THYMIDINE-5'- DIPHOSPHATE'>TYD</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| Line 31: | Line 31: | ||
[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 12:03:11 2008'' |
Revision as of 10:03, 23 March 2008
| |||||||
| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Sun Mar 23 12:03:11 2008
