A LEFT-HANDED PARALLEL BETA-HELIX IN THE STRUCTURE OF UDP-N-ACETYLGLUCOSAMINE ACYLTRANSFERASE

被引：296
作者：
RAETZ, CRH
RODERICK, SL
机构：
[1] ALBERT EINSTEIN COLL MED, DEPT BIOCHEM, BRONX, NY 10461 USA
[2] DUKE UNIV, MED CTR, DEPT BIOCHEM, DURHAM, NC 27710 USA
来源：
SCIENCE | 1995年 / 270卷 / 5238期
关键词：
D O I：
10.1126/science.270.5238.997
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
UDP-N-acetylglucosamine 3-O-acyltransferase (LpxA) catalyzes the transfer of (R)-3-hydroxymyristic acid from its acyl carrier protein thioester to UDP-N-acetylglucosamine. LpxA is the first enzyme in the lipid A biosynthetic pathway and is a target for the design of antibiotics. The x-ray crystal structure of LpxA has been determined to 2.6 angstrom resolution and reveals a domain motif composed of parallel beta strands, termed a left-handed parallel beta helix (L beta H). This unusual fold displays repeated violations of the protein folding constraint requiring right-handed crossover connections between strands of parallel beta sheets and may be present in other enzymes that share amino acid sequence homology to the repeated hexapeptide motif of LpxA.
引用
收藏
页码：997 / 1000
页数：4
相关论文
共 33 条
1234