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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structure of the Rhizomucor miehei aspartic proteinase complexed with the inhibitor pepstatin A at 2.7 A resolution.
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Structure of the Rhizomucor miehei aspartic proteinase complexed with the inhibitor pepstatin A at 2.7 A resolution.

机译：结构的Rhizomucor miehei天冬氨酸的蛋白酶抑制剂抑肽素包裹着一个分辨率为2.7。

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摘要

Crystals of Rhizomucor miehei aspartic proteinase (RMP) complexed with pepstatin A grew in the orthorhombic space group P212121 and were isomorphous to native RMP crystals. The unit-cell dimensions are a = 41.52, b = 50.82, c = 172.71 A. There is one RMP-pepstatin A complex per asymmetric unit. The structure of the RMP-pepstatin A complex has been refined to a crystallographic R value of 19.3% and an Rfree value of 28.0% at 2.7 A resolution. A pepstatin A molecule fits into the large substrate-binding cleft between the two domains of RMP in an extended conformation up to the alanine residue at the P2' position. The dipeptide analogue statine residue at the P3'-P4' position forms an inverse gamma-turn (P3'-P1') with the statine residue at the P1-P1' position and its leucyl side chain binds back into the S1' subsite. The inhibitor interacts with the residues of the substrate-binding pocket by both hydrogen bonds and hydrophobic interactions. The hydroxyl group of the statine residue at the P1-P1' position forms hydrogen bonds with both catalytic aspartate residues (Asp38 and Asp237). This conformation mimics the expected transition state of the enzyme-substrate interaction. The binding of the inhibitor to the enzyme does not produce large distortions of the active site. No domain movement was observed compared with the native enzyme structure. However, the surface-flap region (residues 82-88) undergoes a conformational change, moving toward the inhibitor and becoming rigid owing to the formation of hydrogen bonds with the inhibitor. B-factor calculations of the two domains suggest that the C-terminal domain becomes more rigid in the complex than in the native structure.
机译：晶体的Rhizomucor miehei天冬氨酸的蛋白酶(RMP)包裹着抑肽素了斜方晶系的空间群P212121和同形本机RMP晶体。尺寸是一个= 41.52,b = 50.82, c = 172.71答:有一个RMP-pepstatin复杂的每不对称单元。RMP-pepstatin复杂被精炼和一个Rfree晶体R值的19.3%28.0%至2.7一项决议的价值。适合大型substrate-binding分子RMP的两个域之间的间隙扩展构象丙氨酸残基在P2的位置。statine残留在P3 p4的位置形成了逆gamma-turn statine (P3“p1”)残留在P1-P1的位置及其leucyl侧链结合回S1 '子站。抑制剂与残留的交互由氢键substrate-binding口袋和疏水相互作用。statine残渣的P1-P1的位置与催化之间形成氢键天冬氨酸残基(Asp38和Asp237)。构象模拟预期的过渡态es的交互。抑制剂的酶不能产生大扭曲的活性部位。运动是观察与本机酶的结构。区域(残留物,82 - 88年)经历构象变化,向移动抑制剂和成为刚性由于形成氢键的抑制剂。b因子计算两个领域的建议c端领域变得更加严格本机结构复杂。

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