真核生物鸟氨酸脱羧酶空间结构的建模
Modeling of the spatial structure of eukaryotic ornithine decarboxylases.
作者信息
Grishin N V, Phillips M A, Goldsmith E J
机构信息
Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas 75235, USA.
出版信息
Protein Sci. 1995 Jul;4(7):1291-304. doi: 10.1002/pro.5560040705.
Abstract
We used sequence and structural comparisons to determine the fold for eukaryotic ornithine decarboxylase, which we found is related to alanine racemase. These enzymes have no detectable sequence identity with any protein of known structure, including three pyridoxal phosphate-utilizing enzymes. Our studies suggest that the N-terminal domain of ornithine decarboxylase folds into a beta/alpha-barrel. Through the analysis of known barrel structures we developed a topographic model of the pyridoxal phosphate-binding domain of ornithine decarboxylase, which predicts that the Schiff base lysine and a conserved glycine-rich sequence both map to the C-termini of the beta-strands. Other residues in this domain that are likely to have essential roles in catalysis, substrate, and cofactor binding were also identified, suggesting that this model will be a suitable guide to mutagenic analysis of the enzyme mechanism.
摘要
我们利用序列和结构比较来确定真核鸟氨酸脱羧酶的折叠方式，发现它与丙氨酸消旋酶有关。这些酶与任何已知结构的蛋白质都没有可检测到的序列同一性，包括三种利用磷酸吡哆醛的酶。我们的研究表明，鸟氨酸脱羧酶的N端结构域折叠成一个β/α桶状结构。通过对已知桶状结构的分析，我们建立了鸟氨酸脱羧酶磷酸吡哆醛结合结构域的拓扑模型，该模型预测席夫碱赖氨酸和一个保守的富含甘氨酸的序列都位于β链的C端。该结构域中其他可能在催化、底物和辅因子结合中起重要作用的残基也被确定，这表明该模型将为酶作用机制的诱变分析提供合适的指导。
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