Blue copper proteins: A comparative analysis of their molecular interaction properties

被引:104
|
作者
De Rienzo, F
Gabdoulline, RR
Menziani, MC
Wade, RC
机构
[1] European Mol Biol Lab, D-69012 Heidelberg, Germany
[2] Univ Modena, Dipartimento Chim, I-41100 Modena, Italy
[3] Russian Acad Sci, Inst Math Problems Biol, Pushchino 142292, Moscow Region, Russia
关键词
blue copper proteins; electrostatic potential; electron transfer; hydrophobic potential; protein-protein interactions; redox proteins; similarity index;
D O I
10.1110/ps.9.8.1439
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
Blue copper proteins are type-I copper containing redox proteins whose role is to shuttle electrons from an electron donor to an electron acceptor in bacteria and plants. A large amount of experimental data is available on blue copper proteins; however, their functional characterization is hindered by the complexity of redox processes in biological systems. We describe here the application of a semiquantitative method based on a comparative analysis of molecular interaction fields to gain insights into the recognition properties of blue copper proteins. Molecular electrostatic and hydrophobic potentials were computed and compared for a set of 33 experimentally-determined structures of proteins from seven blue copper subfamilies, and the results were quantified by means of similarity indices. The analysis provides a classification of the blue copper proteins and shows that (1) comparison of the molecular electrostatic potentials provides useful information complementary to that highlighted by sequence analysis; (2) similarities in recognition properties can be detected for proteins belonging to different subfamilies, such as amicyanins and pseudoazurins, that may be isofunctional proteins; (3) dissimilarities in interaction properties, consistent with experimentally different binding specificities, may be observed between proteins belonging to the same subfamily, such as cyanobacterial and eukaryotic plastocyanins; (4) proteins with low sequence identity, such as azurins and pseudoazurins, can have sufficient similarity to bind to similar electron donors and accepters while having different binding specificity profiles.
引用
收藏
页码:1439 / 1454
页数:16
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