Crystal structure of recombinant chicken triosephosphate isomerase-phosphoglycolohydroxamate complex at 1.8-A resolution.
Crystal structure of recombinant chicken triosephosphate isomerase-phosphoglycolohydroxamate complex at 1.8-A resolution.
复制标题
重组鸡磷酸三糖异构酶-磷酸乙二醇异羟肟酸复合物的晶体结构，分辨率为 1.8-A。
DOI：
10.1021/bi00176a012
复制
发表时间：
1994
期刊：
影响因子：
2.9
通讯作者：
Ringe,D
中科院分区：
文献类型：
--
作者：
Zhang,Z;Sugio,S;Komives,EA;Liu,KD;Knowles,JR;Petsko,GA;Ringe,D
1993年12月13日接收的修订版Mandarin pt®摘要：重组鸡磷酸丙糖异构酶（TIM，EC 5.3）的晶体结构。1.1)与中间体类似物PGH形成络合物，用分子置换法进行了解析，在1.8-A分辨率下，R因子为18.5%。结构基本上与酵母TIM-PGH复合物的结构相同[Davenport，RC，et al.（1991）Biochemistry 30，5821 - 5826]，其在较早时测定并以可比的分辨率精制。这种身份延伸到高能量构象的活性位点残基赖氨酸13和丝氨酸211，以及几个结合水分子的位置，保留在活性位点时，PGH的约束。与未复合的鸡TIM结构的比较表明，当PGH结合时，催化碱Glul 65移动了几个埃。这种运动可能会提供一个触发较大的构象变化，一个7 A，在一个环附近的活性位点，向下折叠像一个盖子，以屏蔽结合的抑制剂和催化剂残留物接触散装溶剂。这些相同的构象变化被视为在结晶酵母TIM结合PGH后，他们在这里出现在一个不同的晶体形式的TIM消除了可能性，他们是一个人工晶体包装。
Revised Manuscript Received December 13, 1993® abstract: The crystal structure of recombinant chicken triosephosphateisomerase (TIM, EC 5.3. 1.1) complexed with the intermediate analogue phosphoglycolohydroxamate (PGH) has been solvedby the method of molecular replacement and refined to an R-factor of 18.5% at 1.8-A resolution. The structure is essentially identical to thatof the yeast TIM-PGH complex [Davenport, RC, et al.(1991) Biochemistry 30, 5821-5826] determined earlier and refined at comparable resolution. This identity extends to the high-energy conformations of the active-site residues Lys 13 and Ser211, as well as the positions of several bound water molecules that are retained in the active site when PGH is bound. Comparisonwith the structure of uncomplexed chicken TIM shows that the catalytic base, Glul65, moves several angstroms when PGH binds. This movement may provide a trigger for a larger conformational change, one of 7 A, in a loop near the active site, which folds down like a lid to shield the bound inhibitor and catalytic residues from contact with bulk solvent. These same conformational changes were seen in crystalline yeast TIM upon binding of PGH; their occurrence here in a different crystal form of TIM eliminates the possibility that they are an artifact of crystal packing.