3G0T

Crystal structure of putative aspartate aminotransferase (NP_905498.1) from Porphyromonas gingivalis W83 at 1.75 A resolution

3G0T の概要

• エントリーDOI: 10.2210/pdb3g0t/pdb
• 分子名称: Putative aminotransferase, SODIUM ION, CHLORIDE ION, ... (6 entities in total)
• 機能のキーワード: np_905498.1, putative aspartate aminotransferase, structural genomics, joint center for structural genomics, jcsg, protein structure initiative, psi-2, aminotransferase, transferase
• 由来する生物種: Porphyromonas gingivalis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 102770.83

構造登録者

Joint Center for Structural Genomics (JCSG) (登録日: 2009-01-28, 公開日: 2009-02-10, 最終更新日: 2023-02-01)

主引用文献

Fleischman, N.M.,Das, D.,Kumar, A.,Xu, Q.,Chiu, H.J.,Jaroszewski, L.,Knuth, M.W.,Klock, H.E.,Miller, M.D.,Elsliger, M.A.,Godzik, A.,Lesley, S.A.,Deacon, A.M.,Wilson, I.A.,Toney, M.D.
Molecular characterization of novel pyridoxal-5'-phosphate-dependent enzymes from the human microbiome.
Protein Sci., 23:1060-1076, 2014

PubMed Abstract: Pyridoxal-5'-phosphate or PLP, the active form of vitamin B6, is a highly versatile cofactor that participates in a large number of mechanistically diverse enzymatic reactions in basic metabolism. PLP-dependent enzymes account for ∼1.5% of most prokaryotic genomes and are estimated to be involved in ∼4% of all catalytic reactions, making this an important class of enzymes. Here, we structurally and functionally characterize three novel PLP-dependent enzymes from bacteria in the human microbiome: two are from Eubacterium rectale, a dominant, nonpathogenic, fecal, Gram-positive bacteria, and the third is from Porphyromonas gingivalis, which plays a major role in human periodontal disease. All adopt the Type I PLP-dependent enzyme fold and structure-guided biochemical analysis enabled functional assignments as tryptophan, aromatic, and probable phosphoserine aminotransferases.

PubMed: 24888348
DOI: 10.1002/pro.2493

実験手法

X-RAY DIFFRACTION (1.75 Å)