1YTE

Crystal structure of a nicotinate phosphoribosyltransferase from Thermoplasma acidophilum, phosphoribosylpyrophosphate bound structure

1YTE の概要

• エントリーDOI: 10.2210/pdb1yte/pdb
• 関連するPDBエントリー: 1YTD 1YTK
• 分子名称: nicotinate phosphoribosyltransferase from Thermoplasma acidophilum, 1-ALPHA-PYROPHOSPHORYL-2-ALPHA,3-ALPHA-DIHYDROXY-4-BETA-CYCLOPENTANE-METHANOL-5-PHOSPHATE (3 entities in total)
• 機能のキーワード: nicotinate phosphoribosyltransferase, type ii phosphoribosyltransferase, zinc-knuckle motif, structural genomics, psi, protein structure initiative, berkeley structural genomics center, bsgc, transferase
• 由来する生物種: Thermoplasma acidophilum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 44083.20

構造登録者

Shin, D.H.,Berkeley Structural Genomics Center (BSGC) (登録日: 2005-02-10, 公開日: 2005-03-08, 最終更新日: 2024-10-16)

主引用文献

Shin, D.H.,Oganesyan, N.,Jancarik, J.,Yokota, H.,Kim, R.,Kim, S.H.
Crystal structure of a nicotinate phosphoribosyltransferase from Thermoplasma acidophilum.
J.Biol.Chem., 280:18326-18335, 2005

PubMed Abstract: We have determined the crystal structure of nicotinate phosphoribosyltransferase from Themoplasma acidophilum (TaNAPRTase). The TaNAPRTase has three domains, an N-terminal domain, a central functional domain, and a unique C-terminal domain. The crystal structure revealed that the functional domain has a type II phosphoribosyltransferase fold that may be a common architecture for both nicotinic acid and quinolinic acid (QA) phosphoribosyltransferases (PRTase) despite low sequence similarity between them. Unlike QAPRTase, TaNAPRTase has a unique extra C-terminal domain containing a zinc knuckle-like motif containing 4 cysteines. The TaNAPRTase forms a trimer of dimers in the crystal. The active site pocket is formed at dimer interfaces. The complex structures with phosphoribosylpyrophosphate (PRPP) and nicotinate mononucleotide (NAMN) showed, surprisingly, that functional residues lining on the active site of TaNAPRTase are quite different from those of QAPRTase, although their substrates are quite similar to each other. The phosphate moiety of PRPP and NAMN is anchored to the phosphate-binding loops formed by backbone amides, as found in many alpha/beta barrel enzymes. The pyrophosphate moiety of PRPP is located at the entrance of the active site pocket, whereas the nicotinate moiety of NAMN is located deep inside. Interestingly, the nicotinate moiety of NAMN is intercalated between highly conserved aromatic residues Tyr(21) and Phe(138). Careful structural analyses combined with other NAPRTase sequence subfamilies reveal that TaNAPRTase represents a unique sequence subfamily of NAPRTase. The structures of TaNAPRTase also provide valuable insight for other sequence subfamilies such as pre-B cell colony-enhancing factor, known to have nicotinamide phosphoribosyltransferase activity.

PubMed: 15753098
DOI: 10.1074/jbc.M501622200

実験手法

X-RAY DIFFRACTION (2.75 Å)