1TKS
Crystal structure of 3,4-Dihydroxy-2-butanone 4-phosphate Synthase of Candida albicans
1TKS の概要
| エントリーDOI | 10.2210/pdb1tks/pdb |
| 関連するPDBエントリー | 1TKU |
| 分子名称 | 3,4-dihydroxy-2-butanone 4-phosphate synthase (2 entities in total) |
| 機能のキーワード | candida albicans, riboflavin biosynthesis, 3, 4-dihydroxy-2-butanone 4-phosphate synthase, crystal structure synthetic gene, isomerase |
| 由来する生物種 | Candida albicans |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 45369.96 |
| 構造登録者 | Echt, S.,Bauer, S.,Steinbacher, S.,Huber, R.,Bacher, A.,Fischer, M. (登録日: 2004-06-09, 公開日: 2004-09-07, 最終更新日: 2023-08-23) |
| 主引用文献 | Echt, S.,Bauer, S.,Steinbacher, S.,Huber, R.,Bacher, A.,Fischer, M. Potential anti-infective targets in pathogenic yeasts: structure and properties of 3,4-dihydroxy-2-butanone 4-phosphate synthase of Candida albicans. J.Mol.Biol., 341:1085-1096, 2004 Cited by PubMed Abstract: A synthetic gene specifying a putative 3,4-dihydroxy-2-butanone 4-phosphate synthase of Candida albicans directed the synthesis of a 22.5 kDa peptide in a recombinant Escherichia coli strain. The recombinant protein was purified to apparent homogeneity by two chromatographic steps and was shown to catalyze the formation of L-3,4-dihydroxy-2-butanone 4-phosphate from ribulose 5-phosphate at a rate of 332 nmol mg(-1) min(-1). Hydrodynamic studies indicated a native molecular mass of 41 kDa in line with a homodimer structure. The protein was crystallized in its apoform. Soaking yielded crystals in complex with the substrate ribulose 5-phosphate. The structures were solved at resolutions of 1.6 and 1.7 angstroms, respectively, using 3,4-dihydroxy-2-butanone 4-phosphate synthase of E. coli for molecular replacement. Structural comparison with the orthologs of Magnaporthe grisea and Methanococcus jannaschii revealed a hitherto unknown conformation of the essential acidic active-site loop. PubMed: 15328619DOI: 10.1016/j.jmb.2004.06.053 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.6 Å) |
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