3O61
Structure of the E100A E.coli GDP-mannose hydrolase (yffh) in complex with GDP-mannose and Mg++
3O61 の概要
| エントリーDOI | 10.2210/pdb3o61/pdb |
| 関連するPDBエントリー | 3O52 3O69 3O6Z |
| 分子名称 | GDP-mannose pyrophosphatase nudK, GUANOSINE-5'-DIPHOSPHATE-ALPHA-D-MANNOSE, MAGNESIUM ION, ... (6 entities in total) |
| 機能のキーワード | nudix, gdp_mannose, hydrolase, biofilm |
| 由来する生物種 | Escherichia coli |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 89462.41 |
| 構造登録者 | |
| 主引用文献 | Boto, A.N.,Xu, W.,Jakoncic, J.,Pannuri, A.,Romeo, T.,Bessman, M.J.,Gabelli, S.B.,Amzel, L.M. Structural studies of the Nudix GDP-mannose hydrolase from E. coli reveals a new motif for mannose recognition. Proteins, 79:2455-2466, 2011 Cited by PubMed Abstract: The Nudix hydrolase superfamily, characterized by the presence of the signature sequence GX(5)EX(7)REUXEEXGU (where U is I, L, or V), is a well-studied family in which relations have been established between primary sequence and substrate specificity for many members. For example, enzymes that hydrolyze the diphosphate linkage of ADP-ribose are characterized by having a proline 15 amino acids C-terminal of the Nudix signature sequence. GDPMK is a Nudix enzyme that conserves this characteristic proline but uses GDP-mannose as the preferred substrate. By investigating the structure of the GDPMK alone, bound to magnesium, and bound to substrate, the structural basis for this divergent substrate specificity and a new rule was identified by which ADP-ribose pyrophosphatases can be distinguished from purine-DP-mannose pyrophosphatases from primary sequence alone. Kinetic and mutagenesis studies showed that GDPMK hydrolysis does not rely on a single glutamate as the catalytic base. Instead, catalysis is dependent on residues that coordinate the magnesium ions and residues that position the substrate properly for catalysis. GDPMK was thought to play a role in biofilm formation because of its upregulation in response to RcsC signaling; however, GDPMK knockout strains show no defect in their capacity of forming biofilms. PubMed: 21638333DOI: 10.1002/prot.23069 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.45 Å) |
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