3ACB

Crystal structure of hypoxanthine-guanine phosphoribosyltransferase from Thermus thermophilus HB8

「2YWS」から置き換えられました

3ACB の概要

• エントリーDOI: 10.2210/pdb3acb/pdb
• 関連するPDBエントリー: 3ACC 3ACD
• 分子名称: Hypoxanthine-guanine phosphoribosyltransferase, 1,4-DIETHYLENE DIOXIDE (3 entities in total)
• 機能のキーワード: rossmann fold, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, glycosyltransferase, transferase
• 由来する生物種: Thermus thermophilus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20369.47

構造登録者

Kanagawa, M.,Baba, S.,Hirotsu, K.,Kuramitsu, S.,Yokoyama, S.,Kawai, G.,Sampei, G.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2009-12-30, 公開日: 2010-02-09, 最終更新日: 2023-11-01)

主引用文献

Kanagawa, M.,Baba, S.,Ebihara, A.,Shinkai, A.,Hirotsu, K.,Mega, R.,Kim, K.,Kuramitsu, S.,Sampei, G.,Kawai, G.
Structures of hypoxanthine-guanine phosphoribosyltransferase (TTHA0220) from Thermus thermophilus HB8.
Acta Crystallogr.,Sect.F, 66:893-898, 2010

PubMed Abstract: Hypoxanthine-guanine phosphoribosyltransferase (HGPRTase), which is a key enzyme in the purine-salvage pathway, catalyzes the synthesis of IMP or GMP from alpha-D-phosphoribosyl-1-pyrophosphate and hypoxanthine or guanine, respectively. Structures of HGPRTase from Thermus thermophilus HB8 in the unliganded form, in complex with IMP and in complex with GMP have been determined at 2.1, 1.9 and 2.2 A resolution, respectively. The overall fold of the IMP complex was similar to that of the unliganded form, but the main-chain and side-chain atoms of the active site moved to accommodate IMP. The overall folds of the IMP and GMP complexes were almost identical to each other. Structural comparison of the T. thermophilus HB8 enzyme with 6-oxopurine PRTases for which structures have been determined showed that these enzymes can be tentatively divided into groups I and II and that the T. thermophilus HB8 enzyme belongs to group I. The group II enzymes are characterized by an N-terminal extension with additional secondary elements and a long loop connecting the second alpha-helix and beta-strand compared with the group I enzymes.

PubMed: 20693661
DOI: 10.1107/S1744309110023079

実験手法

X-RAY DIFFRACTION (2.06 Å)