1G97

S.PNEUMONIAE GLMU COMPLEXED WITH UDP-N-ACETYLGLUCOSAMINE AND MG2+

1G97 の概要

• エントリーDOI: 10.2210/pdb1g97/pdb
• 関連するPDBエントリー: 1G95
• 分子名称: N-ACETYLGLUCOSAMINE-1-PHOSPHATE URIDYLTRANSFERASE, MAGNESIUM ION, SODIUM ION, ... (5 entities in total)
• 機能のキーワード: glmu, acetyltransferase, uridyltransferase, pyrophosphorylase, left-handed beta-sheet helix, trimer, magnesium, udp-n-acetylglucosamine, transferase
• 由来する生物種: Streptococcus pneumoniae
• 細胞内の位置: Cytoplasm: Q97R46
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 50053.04

構造登録者

Kostrewa, D.,D'Arcy, A.,Kamber, M. (登録日: 2000-11-22, 公開日: 2001-05-22, 最終更新日: 2023-08-09)

主引用文献

Kostrewa, D.,D'Arcy, A.,Takacs, B.,Kamber, M.
Crystal structures of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase, GlmU, in apo form at 2.33 A resolution and in complex with UDP-N-acetylglucosamine and Mg(2+) at 1.96 A resolution.
J.Mol.Biol., 305:279-289, 2001

PubMed Abstract: N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU) is an essential bacterial enzyme with both an acetyltransferase and a uridyltransferase activity which have been mapped to the C-terminal and N-terminal domains, respectively. GlmU performs the last two steps in the synthesis of UDP-N-acetylglucosamine (UDP-GlcNAc), which is an essential precursor in both the peptidoglycan and the lipopolysaccharide metabolic pathways. GlmU is therefore an attractive target for potential antibiotics. Knowledge of its three-dimensional structure would provide a basis for rational drug design. We have determined the crystal structures of Streptococcus pneumoniae GlmU (SpGlmU) in apo form at 2.33 A resolution, and in complex with UDP-N-acetyl glucosamine and the essential co-factor Mg(2+) at 1.96 A resolution. The protein structure consists of an N-terminal domain with an alpha/beta-fold, containing the uridyltransferase active site, and a C-terminal domain with a long left-handed beta-sheet helix (LbetaH) domain. An insertion loop containing the highly conserved sequence motif Asn-Tyr-Asp-Gly protrudes from the left-handed beta-sheet helix domain. In the crystal, S. pneumoniae GlmU forms exact trimers, mainly through contacts between left-handed beta-sheet helix domains. UDP-N-acetylglucosamine and Mg(2+) are bound at the uridyltransferase active site, which is in a closed form. We propose a uridyltransferase mechanism in which the activation energy of the double negatively charged phosphorane transition state is lowered by charge compensation of Mg(2+) and the side-chain of Lys22.

PubMed: 11124906
DOI: 10.1006/jmbi.2000.4296

実験手法

X-RAY DIFFRACTION (1.96 Å)