Functional diversity of the phosphoglucomutase superfamily: structural implications

被引:22
作者
Levin, S
Almo, SC
Satir, BH
机构
[1] Albert Einstein Coll Med, Dept Anat, Bronx, NY 10461 USA
[2] Albert Einstein Coll Med, Dept Biol Struct, Bronx, NY 10461 USA
[3] Albert Einstein Coll Med, Dept Biochem, Bronx, NY 10461 USA
来源
PROTEIN ENGINEERING | 1999年 / 12卷 / 09期
关键词
aciculin; parafusin; phosphoglucomutase; protein superfamily;
D O I
10.1093/protein/12.9.737
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Three-dimensional structural models of three members of the phosphoglucomutase (PGM) superfamily, parafusin, phosphoglucomutase-related protein and sarcoplasmic reticulum phosphoglucomutase, were constructed by homology modeling based on the known crystal structure of rabbit muscle phosphoglucomutase. Parafusin, phosphoglucomutase-related protein and sarcoplasmic reticulum phosphoglucomutase each have 50% or more identity with rabbit muscle phosphoglucomutase at the amino acid level and all are reported to exhibit no or minor phosphoglucomutase activity. There are four major insertions and two deletions in the parafusin sequence relative to PGM, all of which are located in surface-exposed loops connecting secondary structural elements. The remaining amino acid substitutions are distributed throughout the sequence and are not predicted to alter the polypeptide fold. Parafusin contains a putative protein kinase C site located on a surface loop in domain II that is not present in the homologs, Although the general domain structure and the active site of rabbit muscle phosphoglucomutase are preserved in the model of phosphoglucomutase-related protein, a major structural difference is likely to occur in domain 1 due to the absence of 55 amino acid residues in PGM-RP, This deletion predicts the loss of three alpha-helices and one beta-strand from an anti-parallel beta-sheet in this domain as compared with the rabbit muscle phosphoglucomutase.
引用
收藏
页码:737 / 746
页数:10
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