通过同源性建模并经定点诱变验证的丝氨酸羟甲基转移酶结构。
The structure of serine hydroxymethyltransferase as modeled by homology and validated by site-directed mutagenesis.
作者信息
Pascarella S, Angelaccio S, Contestabile R, Delle Fratte S, Di Salvo M, Bossa F
机构信息
Dipartimento di Scienze Biochimiche A. Rossi Fanelli and Centro di Biologia Molecolare del CNR, Università La Sapienza, Roma, Italy.
出版信息
Protein Sci. 1998 Sep;7(9):1976-82. doi: 10.1002/pro.5560070913.
Abstract
We describe a model for the three-dimensional structure of E. coli serine hydroxymethyltransferase based on its sequence homology with other PLP enzymes of the alpha-family and whose tertiary structures are known. The model suggests that certain amino acid residues at the putative active site of the enzyme can adopt specific roles in the catalytic mechanism. These proposals were supported by analysis of the properties of a number of site-directed mutants. New active site features are also proposed for further experimental testing.
摘要
我们基于大肠杆菌丝氨酸羟甲基转移酶与α-家族其他磷酸吡哆醛（PLP）酶的序列同源性及其已知的三级结构，描述了该酶的三维结构模型。该模型表明，酶的假定活性位点处的某些氨基酸残基在催化机制中可发挥特定作用。这些提议得到了对许多定点突变体性质分析的支持。还提出了新的活性位点特征以供进一步实验验证。
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