1HMP

THE CRYSTAL STRUCTURE OF HUMAN HYPOXANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE WITH BOUND GMP

1HMP の概要

• エントリーDOI: 10.2210/pdb1hmp/pdb
• 分子名称: HYPOXANTHINE GUANINE PHOSPHORIBOSYL-TRANSFERASE, GUANOSINE-5'-MONOPHOSPHATE (3 entities in total)
• 機能のキーワード: transferase (glycosyltransferase)
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 49688.88

構造登録者

Eads, J.C.,Scapin, G.,Xu, Y.,Grubmeyer, C.,Sacchettini, J.C. (登録日: 1994-06-03, 公開日: 1995-06-03, 最終更新日: 2024-02-07)

主引用文献

Eads, J.C.,Scapin, G.,Xu, Y.,Grubmeyer, C.,Sacchettini, J.C.
The crystal structure of human hypoxanthine-guanine phosphoribosyltransferase with bound GMP.
Cell(Cambridge,Mass.), 78:325-334, 1994

PubMed Abstract: The crystal structure of HGPRTase with bound GMP has been determined and refined to 2.5 A resolution. The enzyme has a core alpha/beta structure resembling the nucleotide-binding fold of dehydrogenases, and a second lobe composed of residues from the amino and carboxy termini. The GMP molecule binds in an anti conformation in a solvent-exposed cleft of the enzyme. Lys-165, which forms a hydrogen bond to O6 of GMP, appears to be critical for determining the specificity for guanine and hypoxanthine over adenine. The location of active site residues also provides evidence for a possible mechanism for general base-assisted HGPRTase catalysis. A rationalization of the effects on stability and activity of naturally occurring single amino acid mutations of HGPRTase is presented, including a discussion of several mutations at the active site that lead to Lesch-Nyhan syndrome.

PubMed: 8044844
DOI: 10.1016/0092-8674(94)90301-8

実験手法

X-RAY DIFFRACTION (2.5 Å)