Question

求大虾翻译，谢谢啊，急用

Structure
The domain structure of GLUD1
Each domain is colored differently - Glu-BD, NAD(P)-BD, antena, the pivot helix. The allosteric regulators are shown as sphere models. This particular structure of GLUD1 is a combination of two X-ray structures - one with a bound GTP (1HWZ) and the second one with a bound ADP (1NQT). Although not real, this structure shows the relative position of the allosteric effectors when bound to GLUD1. NADPH and Glu are shown as well.GLUD1 is a hexamer. The monomer unit has:

1.N-terminal Glu-BD(Binding domain) that is composed mostly of β-strands.
2.NAD-BD - can bind either NAD+ or NADP+.
3.48-residue antenna-like projection that extends from the top of each NAD-BD. The antenna consists of an ascending helix and a descending random coil strand that contains a small α-helix toward the C-terminal end of the strand.
NAD-BD sits on the top of Glu-BD. NAD-BD and Glu-BD form the catalytic cleft. During substrate binding, the NAD-BD moves significantly. This movement has two components, rotating along the long axis of a helix at the back of the NAD-BD, called "the pivot helix", and twisting about the antenna in a clockwise fashion. A comparison of the open and closed conformations of GLUD1 reveals changes in the small helix of the descending strand of the antenna, which seems to recoil as the catalytic cleft opens.[1] Closure of one subunit is associated with distortion of the small helix of the descending strand that is pushed into the antenna of the adjacent subunit. R496 is located on this small helix (see Mutations).

The core structure of the hexamer is a stacked dimer of trimers. Glu-BDs of the monomers are mainly responsible in the build up of the core. The relative position of the monomers is such that the rotation about the pivot helix in each monomer is not restricted. The antennae from three subunits within the trimers wrap around each other and undergo conformational changes as the catalytic cleft opens and closes. The antenna serves as an intersubunit communication conduit during negative cooperativity and allosteric regulation.

Alignment of GLUD1 from various sources, shows that the antenna probably evolved in the protista prior to the formation of purine regulatory sites. This suggests that there is some selective advantage of the antenna itself and that animals evolved new functions for GLUD1 through the addition of allosteric regulation.[2]

GLUD1 can form long fibers by end to end association of the hexamers. The polimerization is unrelated to the catalytic activity, but probably has an important role such as formation of multienzyme comolexes.

GLUD1 has two co-enzyme binding sites: one in the NAD-BD that is able to bind ether NAD+ or NADP+ and is directly involved in the catalytic process, and a second one, that has regulatory function, lying directly under the pivot helix, that can bind ADP, NAD+, or NADH, but does not bind NADPH well.[3]

Answer 1

结构
GLUD1域结构
每个“域”Glu-BD不同——色彩,和(P),-BD枢纽,antena螺旋。别构的监管机构表现为球面模型。这个特殊的结构是GLUD1联合使用两种x射线结构约束——一种GTP(1HWZ)和第二绑定的腺(1NQT)。虽然不是真实的,该结构向观众展现构的相对位置时,一定要GLUD1相应。结果图谱和NADPH。GLUD1是一个hexamer。单体单元有:
1。N-terminal Glu-BD(结合域),其中大部分是β-strands。
2。NAD-BD——可以强迫要么和+或NADP间+。
3.48-residue antenna-like投影延伸到上方的每一个NAD-BD。天线由一个提升螺旋和递减,它包含一个随机线圈条小α-helix c端年底向困。 NAD-BD坐在Glu-BD的顶端。NAD-BD和Glu-BD形成催化裂。在NAD-BD移动的约束力,基质显著下降。这个动作有两个组成部分、旋转沿长轴螺旋的NAD-BD的后面,称为“轴螺旋”,扭顺时针方向旋转天线的时尚。比较开启和关闭的构象变化GLUD1揭示了在小螺旋下降的线的天线,这看上去反冲催化的分裂就打开了。越过打开[1]有关关闭一个十分失真,小螺旋的一被推入上去,十分的相邻天线。R496就建在这个小螺旋(见突变)。
核心结构是hexamer堆叠trimers二聚体的。Glu-BDs的单体的主要负责建立的核心。单体的相对位置,其绕轴螺旋在每个单体是不受限制。从三个基天线在trimers披对方,接受的构象变化催化的分裂打开和关闭。天线作为intersubunit通讯管道在负面协同规定。别构从许多不同的来源GLUD1的排列,表明可能形成的天线的形成原生生物:指前嘌呤监督管理的网站。这表明有选择性的微带漏波天线的优点,动物发展了新的本身功能构通过增加GLUD1[2]的规定。
GLUD1可以形成长纤维被端到端的hexamers协会。polimerization的催化活性是无关的,但可能有着非常重要的作用comolexes随著杂粕溢多酶的形成等。
GLUD1有两个介质的:一个在结合位点的NAD-BD,能够把醚和+或NADP间的直接参与+和催化过程和第二一个调节功能,躺下直接轴螺旋,那可以强迫自动数据处理,和+、或NADH,但不代表NADPH[3]。

Answer 2

结构域结构的GLUD1每个域是不同的颜色 - 谷氨酸，屋宇署，抑制NAD（P）-屋宇署的Antena，枢轴螺旋。变构调节器显示为领域模型。这种GLUD1特殊结构是两个X射线结构的结合 - 一个带有约束的GTP（1HWZ）和二磷酸腺苷与约束（1NQT）第二个。虽然不是真实的，这种结构显示了变构效应的相对位置时，必然要GLUD1。 NADPH和谷氨酸显示为well.GLUD1是一种六聚体。单体单位有：1.n的末端谷氨酸-蓝光（绑定域名），它主要是由β-折叠。2.NAD - BD的 - 要么可以绑定或辅酶NAD +的+。3.48残留天线般的投影，从每个辅酶- BD的顶部延伸。该天线由一个螺旋上升和下降无规卷曲链，其中包含一个小型的α-朝链的C末端的螺旋。NAD的，屋宇署就坐在谷氨酸- BD的顶部。 NAD的，屋宇署和Glu - BD的形式催化裂。在底物结合，与NAD - BD的动作明显。这一运动由两部分组成，沿着一个在北美地区，屋宇署回螺旋长轴旋转，所谓的“支点螺旋”，以及对时尚的天线以顺时针扭动。一对GLUD1开启和关闭的构象比较显示在了天线，这似乎反冲的催化裂开降小螺旋链的变化。[1]一亚基与封闭的小螺旋扭曲的关联降链是推入相邻亚基天线。 R496是位于这个小螺旋（见突变）。该六聚体的核心结构是三聚体堆积二聚体。谷氨酸-的BD的单体主要负责在构建核心了。三种单体的相对位置是这样的：关于在每个单体枢轴螺旋转动不限制。从三聚体中的三个亚基触角互相环绕的构象变化，并进行催化裂打开和关闭。该天线可作为在负变构调节intersubunit协同和沟通的渠道。从各种来源GLUD1对准，表明该天线可能在之前的调控位点的形成嘌呤原生动物进化而来的。这表明，有一些选择性天线本身的优势，是动物进化成GLUD1通过增加新的功能变构调节[2]。GLUD1年底可形成长纤维到最终的六聚体协会。该polimerization无关的催化活性，但很可能有一个如多酶comolexes形成的重大作用。GLUD1有两个共同酶结合位点：在NAD - BD的一个是能够结合醚的NAD +或辅酶+，直接在催化过程中所涉及，而第二个，具有调节功能，卧下的支点螺旋直接，二磷酸腺苷，可以结合，NAD +的，或NADH，但不具约束力的NADPH很好。