Structure of the lamprey yolk lipid-protein complex lipovitellin-phosvitin at 2.8 A resolution.

Structure of the lamprey yolk lipid-protein complex lipovitellin-phosvitin at 2.8 A resolution.
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七鳃鳗卵黄脂质-蛋白质复合物脂卵黄蛋白-卵黄高磷蛋白的结构,分辨率为 2.8 A。

DOI:
10.1016/0022-2836(88)90542-6
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发表时间:
1988
影响因子:
5.6
通讯作者:
Banaszak,L
Banaszak,L
中科院分区:
生物学2区
文献类型:
--
作者:
Raag,R;Appelt,K;Xuong,NH;Banaszak,L

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本文用四种重原子衍生物的多重同晶置换法测定了脂质-蛋白质复合物lipovitellin-lavitin的X射线晶体结构。七鳃鳗卵黄脂蛋白是一种二聚体分子,分子量为352,000。单体由三条多肽链组成。最小的是已知的维生素E,具有极高的磷酸丝氨酸含量。单体单元还含有约16%(w/w)的非共价结合的脂质,可能呈单层或双层样构型。在每个单体内是低电子密度的“空腔”或区域。空腔的体积约为68,000立方厘米,据信含有可能处于无序状态的脂质。空腔大致呈圆锥形,两侧排列着七股和八股反向平行的β折叠。空腔的底部远离亚基间界面打开,但似乎通过额外的反平行β-折叠结构与溶剂区域部分封闭。排列在空腔两侧的β-片层被一个由16个相互连接的螺旋组成的两个弯曲层的壳包围。壳层的任一层中的螺旋都大致彼此平行,并且与另一层的所有螺旋反平行。螺旋的连接类似于“超螺旋”,与含有四螺旋束的蛋白质中的连接不同。七鳃鳗卵黄脂蛋白中估计有1300个氨基酸,近1000个丙氨酸残基已被建模为电子密度。其余的残基被认为是无序的。
The X-ray crystallographic structure of the lipid-protein complex lipovitellin-phosvitin has been determined with the multiple isomorphous replacement method using four heavyatom derivatives. Lamprey yolk lipovitellin-phosvitin is a dimeric molecule of molecular weight 352,000. The monomer consists of three polypeptide chains. The smallest is known as phosvitin and has an extremely high phosphoserine content. The monomeric unit also contains about 16%(w w) of non-covalently bound lipid, probably in a monolayer or bilayer-like configuration. Within each monomer is a “cavity” or region of low electron density. The cavity has a volume of about 68,000 Å 3 and is believed to contain the lipid in a presumably disordered state. The cavity is roughly conical in shape and is lined on two sides by seven and eight-stranded antiparallel β-sheets. The base of the cavity opens away from the intersubunit interface, but appears partially closed off from solvent regions by additional antiparallel β-sheet structure. The β-sheets lining the sides of the cavity are surrounded by a shell of two curved layers of 16 interconnected helices. The helices in either layer of the shell are all roughly parallel to each other and antiparallel to all of the helices of the other layer. The connectivity of the helices resembles a “superhelix” and is different from the connectivities seen in proteins containing four-helix bundles. There are an estimated 1300 amino acids in lamprey lipovitellin-phosvitin and almost 1000 alanine residues have been modeled into electron density. The remaining residues are assumed to be disordered.
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