1V9A

Crystal structure of Uroporphyrin-III C-methyl transferase from Thermus thermophilus complexed with S-adenyl homocysteine

1V9A の概要

• エントリーDOI: 10.2210/pdb1v9a/pdb
• 関連するPDBエントリー: 1VA0
• 分子名称: Uroporphyrin-III C-methyltransferase, CITRATE ANION, S-ADENOSYL-L-HOMOCYSTEINE, ... (4 entities in total)
• 機能のキーワード: transferase, structural genomics, riken structural genomics/proteomics initiative, rsgi
• 由来する生物種: Thermus thermophilus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 53434.00

構造登録者

Rehse, P.H.,Kitao, T.,Tahirov, T.H.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2004-01-23, 公開日: 2005-02-01, 最終更新日: 2023-10-25)

主引用文献

Rehse, P.H.,Kitao, T.,Tahirov, T.H.
Structure of a closed-form uroporphyrinogen-III C-methyltransferase from Thermus thermophilus.
Acta Crystallogr.,Sect.D, 61:913-919, 2005

PubMed Abstract: Uroporphyrinogen-III C-methyltransferase from Thermus thermophilus is a multifunctional protein responsible for two of the eight S-adenosyl-methionine-dependent methylations of the corrin ring during vitamin B(12) synthesis. The structure of this protein has been solved to 2.0 A resolution in both the apo and cofactor-bound form. The monomer consists of two domains, A and B, each consisting of a five-stranded beta-sheet and two or three alpha-helices, with the cofactor bound at the interface. The biological unit is the dimer found in the asymmetric unit. This dimer is related by a non-crystallographic twofold such that two B domains combine to form a long ten-stranded beta-sheet. When compared with solved related structures, this structure shows clear differences in the region involved in cofactor and substrate binding, affirming the role of several previously implicated residues and questioning others. The solved related structures are characterized by an exposed active site. The T. thermophilus structure has this site restricted by the interaction of a flexible loop structure with a highly conserved residue, suggesting a mechanistic role. This structure represents the ;closed' form of the protein.

PubMed: 15983414
DOI: 10.1107/S0907444905008838

実験手法

X-RAY DIFFRACTION (2 Å)