3-DIMENSIONAL STRUCTURE OF THE ALKALINE PROTEASE OF PSEUDOMONAS-AERUGINOSA - A 2-DOMAIN PROTEIN WITH A CALCIUM-BINDING PARALLEL-BETA ROLL MOTIF
3-DIMENSIONAL STRUCTURE OF THE ALKALINE PROTEASE OF PSEUDOMONAS-AERUGINOSA - A 2-DOMAIN PROTEIN WITH A CALCIUM-BINDING PARALLEL-BETA ROLL MOTIF
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DOI：
10.1002/j.1460-2075.1993.tb06009.x
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发表时间：
1993-09-01
期刊：
影响因子：
11.4
通讯作者：
MCKAY, DB
中科院分区：
文献类型：
--
作者：
BAUMANN, U;WU, S;MCKAY, DB
铜绿假单胞菌的碱性蛋白酶，锌金属蛋白酶的三维结构，已解决了1.64埃的分辨率通过多个同晶置换和非晶体学对称性平均之间的不同晶体形式。该分子是细长的，总尺寸为90 x 35 x 25埃;它有两个不同的结构域。N-末端结构域是蛋白水解结构域;它具有总体三级折叠和活性位点锌连接，类似于从欧洲淡水小龙虾中分离的金属蛋白酶--虾红素。C-末端结构域由21链β夹心组成。在该结构域内是一种新的“平行β卷”结构，其中连续的β链以右手螺旋缠绕，并且其中Ca 2+离子通过重复的GGXGXD序列基序结合在链之间的转弯内，该基序在革兰氏阴性菌分泌的不同蛋白质组中发现。
The three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa, a zinc metalloprotease, has been solved to a resolution of 1.64 angstrom by multiple isomorphous replacement and non-crystallographic symmetry averaging between different crystal forms. The molecule is elongated with overall dimensions of 90 x 35 x 25 angstrom; it has two distinct structural domains. The N-terminal domain is the proteolytic domain; it has an overall tertiary fold and active site zinc ligation similar to that of astacin, a metalloprotease isolated from a European freshwater crayfish. The C-terminal domain consists of a 21-strand beta sandwich. Within this domain is a novel 'parallel beta roll' structure in which successive beta strands are wound in a right-handed spiral, and in which Ca2+ ions are bound within the turns between strands by a repeated GGXGXD sequence motif, a motif that is found in a diverse group of proteins secreted by Gram-negative bacteria.