✦ LIBER ✦

T-state Inhibitors of E. coli Aspartate Transcarbamoylase that Prevent the Allosteric Transition †,‡

✍ Scribed by Heng, Sabrina; Stieglitz, Kimberly A.; Eldo, Joby; Xia, Jiarong; Cardia, James P.; Kantrowitz, Evan R.

Book ID: 127304509
Publisher: American Chemical Society
Year: 2006
Tongue: English
Weight: 503 KB
Volume: 45
Category: Article
ISSN: 0006-2960
DOI: 10.1021/bi0601095

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

A Single Amino Acid Substitution in the

A Single Amino Acid Substitution in the Active Site of Escherichia coli Aspartate Transcarbamoylase Prevents the Allosteric Transition

✍ Kimberly A. Stieglitz; Styliani C. Pastra-Landis; Jiarong Xia; Hiro Tsuruta; Eva 📂 Article 📅 2005 🏛 Elsevier Science 🌐 English ⚖ 475 KB

Replacement of Asp-162 by Ala prevents t

Replacement of Asp-162 by Ala prevents the cooperative transition by the substrates while enhancing the effect of the allosteric activator ATP on E. coli aspartate transcarbamoylase

✍ L. Fetler; P. Tauc; D.P. Baker; C.P. Macol; E.R. Kantrowitz; P. Vachette 📂 Article 📅 2002 🏛 Cold Spring Harbor Laboratory Press 🌐 English ⚖ 129 KB

Monitoring the Transition from the T to

Monitoring the Transition from the T to the R State in E. coli Aspartate Transcarbamoylase by X-ray Crystallography: Crystal Structures of the E50A Mutant Enzyme in Four Distinct Allosteric States

✍ Kimberly Stieglitz; Boguslaw Stec; Darren P. Baker; Evan R. Kantrowitz 📂 Article 📅 2004 🏛 Elsevier Science 🌐 English ⚖ 729 KB

Role of Allosteric:Zinc Interdomain Regi

Role of Allosteric:Zinc Interdomain Region of the Regulatory Subunit in the Allosteric Regulation of Aspartate Transcarbamoylase fromEscherichia coli

✍ Vipin K. Rastogi; Rosemarie Swanson; Yasha M. Hartberg; Melinda E. Wales; James 📂 Article 📅 1998 🏛 Elsevier Science 🌐 English ⚖ 495 KB

A single mutation in the regulatory chai

A single mutation in the regulatory chain of Escherichia coli aspartate transcarbamoylase results in an extreme T-state structure

✍ Mark K Williams; Boguslaw Stec; Evan R Kantrowitz 📂 Article 📅 1998 🏛 Elsevier Science 🌐 English ⚖ 553 KB

Effects of the T→R transition on the ele

Effects of the T→R transition on the electrostatic properties of E. coli aspartate transcarbamylase

✍ M. Hariharan; N.M. Allewell 📂 Article 📅 1998 🏛 John Wiley and Sons 🌐 English ⚖ 293 KB 👁 1 views

Aspartate transcarbamylase is a large (310 kD), multisubunit protein that binds substrates cooperatively and undergoes a large change in quaternary structure when substrates bind. The forces that drive this transition are poorly understood. We evaluated the electrostatic component of these forces by