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The three-dimensional structure of shikimate kinase

机译：iki草酸激酶的三维结构

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The three-dimensional structure of shikimate kinase from Erwinia chrysanthemi has been determined by multiple isomorphous replacement. Two models are presented: a high resolution 1.9 Angstrom model and a 2.6 Angstrom model which contains bound Mg-ADP. The enzyme is an alpha/beta protein consisting of a central sheet of five parallel beta-strands flanked by alpha-helices with overall topology similar to adenylate kinase. Evidence is presented that shikimate kinase undergoes major conformational changes on ligand binding. It resembles adenylate kinase in having a P-loop containing core structure and two flexible domains which undergo induced fit movement on substrate binding. The binding of Mg2+ in the active site of shikimate kinase involves direct interaction with two protein side-chains which is different from the situation found in adenylate kinase. Shikimate kinase has a readily identifiable Walker A-motif and a recognisable but modified Walker B-motif. Comparison of shikimate kinase to adenylate kinase has led to the identification of an adenine-binding motif (I/VDAXQ/NXP). Difference Fourier calculations have revealed the shikimate binding site which corresponds to the location of the AMP-binding site in adenylate kinase. A model for shikimate-binding is presented. (C) 1998 Academic Press Limited. [References: 63]
机译：菊花欧文氏菌的sh草酸激酶的三维结构已通过多次同构置换确定。提出了两种模型：高分辨率的1.9埃模型和包含结合的Mg-ADP的2.6埃模型。该酶是一种α/β蛋白，由五个平行的β链的中央薄片组成，中间是两个侧面的α-螺旋，其总体拓扑类似于腺苷酸激酶。证据表明sh草酸激酶在配体结合上发生主要构象变化。它类似于腺苷酸激酶，具有一个包含核心结构的P环和两个柔性结构域，这些结构域在底物结合后经历诱导的运动。 Mg2 +在sh草酸激酶活性位点的结合涉及与两个蛋白质侧链的直接相互作用，这与腺苷酸激酶中的情况不同。 Shikimate激酶具有易于识别的Walker A-基序和可识别但经过修饰的Walker B-基序。 iki草酸酯激酶与腺苷酸激酶的比较已导致鉴定出腺嘌呤结合基序（I / VDAXQ / NXP）。傅立叶差的计算已经揭示sh草酸酯结合位点，其对应于腺苷酸激酶中AMP结合位点的位置。提出了sh酸酯结合的模型。 （C）1998 Academic Press Limited。 [参考：63]

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