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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >The structure of substrate-free microbial ribonuclease binase and of its complexes with 3'GMP and sulfate ions.
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The structure of substrate-free microbial ribonuclease binase and of its complexes with 3'GMP and sulfate ions.

机译：substrate-free微生物的结构核糖核酸酶binase及其复合物3 'gmp和硫酸盐离子。

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摘要

The structures of Bacillus intermedius ribonuclease (binase), an extracellular 109-residue enzyme, and its complexes with 3'GMP and sulfate ions were solved at 1.65 and 2.0 A, respectively. The structures were refined using REFMAC. The crystal of free binase belongs to the space group C2, whereas the crystals of complexes belong to the space group P2(1)2(1)2(1). In both crystal lattices the asymmetric unit contains two molecules which form an identical dimer. The structure of the dimer is such that only one of its subunits can bind the nucleotide in the 3'GMP-binase complex, where the guanyl base is located in the recognition loop of the enzyme. In both binase complex structures the phosphate group of 3'GMP or one of the sulfate ions make an electrostatic interaction with the binase molecule at the catalytic site. A second phosphate-binding site was found in the structures of the complexes at the cleft formed by the loop 34-39, the main chain of Arg82 and the side chain of Trp34. Comparison of the complex and unliganded enzyme crystal structures shows that there are some small but distinct differences in the specificity loop (56-62) and in the loops 34-39 and 99-104 associated with the binding of the nucleotide and sulfate ions.
机译：杆菌中间部的结构核糖核酸酶(binase),一个细胞外109 -残留酶,其与3 'gmp复合物和硫酸盐离子被解决在1.65和2.0,分别。REFMAC。空间群C2,而复合物的晶体属于空间群P2(1) 2(1) 2(1)。晶格的不对称单元包含两个分子形成一个相同的二聚体。二聚体结构是这样,只有一个它的子单元可以绑定的核苷酸3 'gmp-binase复杂,甲脒基基地在哪里位于酶的识别循环。binase复杂结构的磷酸组3 'gmp或硫酸盐离子使之一与binase静电相互作用分子催化部位。phosphate-binding网站被发现的结构裂缝形成的复合物的主链的循环34-39 Arg82和Trp34的侧链。复杂和unliganded酶晶体结构显示,有些小但截然不同不同的特异性(56 - 62)和循环在循环34-39和99 - 104的绑定的核苷酸和硫酸盐离子。

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