Direct structural evidence for a concerted allosteric transition in Escherichia coli aspartate transcarbamoylase
about
Structural basis for ordered substrate binding and cooperativity in aspartate transcarbamoylase.Structural classification of zinc fingers: survey and summary.Allosteric regulation of catalytic activity: Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutaseReplacement 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 transcarbamoylaseFrom Genome to Structure and Back Again: A Family Portrait of the TranscarbamylasesA Cooperative Escherichia coli Aspartate Transcarbamoylase without Regulatory Subunits,Structure and mechanisms of Escherichia coli aspartate transcarbamoylaseStructural and kinetic studies on adenylosuccinate lyase from Mycobacterium smegmatis and Mycobacterium tuberculosis provide new insights on the catalytic residues of the enzymeTime Evolution of the Quaternary Structure of Escherichia coli Aspartate Transcarbamoylase upon Reaction with the Natural Substrates and a Slow, Tight-Binding InhibitorX-ray Scattering Studies of Protein Structural Dynamics.Dual allosteric activation mechanisms in monomeric human glucokinase.Allostery and cooperativity in Escherichia coli aspartate transcarbamoylaseAlkaline phosphatase from the hyperthermophilic bacterium T. maritima requires cobalt for activity.Structural model of the R state of Escherichia coli aspartate transcarbamoylase with substrates bound.Interpretation of solution x-ray scattering by explicit-solvent molecular dynamics.Importance of domain closure for the catalysis and regulation of Escherichia coli aspartate transcarbamoylase.The role of intersubunit interactions for the stabilization of the T state of Escherichia coli aspartate transcarbamoylase.Charge neutralization in the active site of the catalytic trimer of aspartate transcarbamoylase promotes diverse structural changes.Quaternary structure of alpha-crustacyanin from lobster as seen by small-angle X-ray scattering.
P2860
Q24530087-8DC80469-6B33-48B3-A96D-E79CE82723CCQ24540502-A6F7B620-1C77-446B-8AE6-AFD1AF36B9C2Q24548465-3AFED0C1-8DEE-463A-9DF6-C75CD6A0CDD1Q24645129-676D9B87-B5FF-4809-B4FC-DC0C3D949F9DQ26798133-FC665773-A67E-4091-AE9F-44686158C2ACQ27663832-015AD868-3EDC-4FA8-8595-42C916026B6CQ27687456-3233C58D-BDE2-466B-9BC9-477DE9EAF8B5Q27689032-C079941E-4A0C-4C05-A199-0DC8446F070AQ29391897-7CCFA783-AD00-49E3-9C5D-4A7D1814DBE6Q30101114-7CBC8196-2581-4832-85EC-3B3155E7E15CQ35748383-44301C02-A4F9-4FDD-A41B-3FE3CF64E942Q36085714-6A2A6899-4B39-40B5-A30C-66A5A5B24BCDQ36639205-4C9A4C06-7D29-4614-826A-B3B6BDAAEBC4Q37287204-8385F2A1-9838-4946-8FD8-F295DA5F5EF6Q40919953-DEFD98E2-4227-4DDF-89EC-A198ED38C9D9Q43997266-124EC132-F801-4F01-AFFC-7FC7302283DFQ44193826-BDDD7FD8-1CA9-44EB-AB7A-E2B9F9CE2A4AQ46699408-D963E7E9-0913-4E79-AB5D-876E7A25CD3AQ50494279-DC054F39-4450-4A61-8EAB-6EF1DF342189
P2860
Direct structural evidence for a concerted allosteric transition in Escherichia coli aspartate transcarbamoylase
description
2001 nî lūn-bûn
@nan
2001 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Direct structural evidence for ...... li aspartate transcarbamoylase
@ast
Direct structural evidence for ...... li aspartate transcarbamoylase
@en
Direct structural evidence for ...... li aspartate transcarbamoylase
@nl
type
label
Direct structural evidence for ...... li aspartate transcarbamoylase
@ast
Direct structural evidence for ...... li aspartate transcarbamoylase
@en
Direct structural evidence for ...... li aspartate transcarbamoylase
@nl
prefLabel
Direct structural evidence for ...... li aspartate transcarbamoylase
@ast
Direct structural evidence for ...... li aspartate transcarbamoylase
@en
Direct structural evidence for ...... li aspartate transcarbamoylase
@nl
P2093
P356
P1476
Direct structural evidence for ...... li aspartate transcarbamoylase
@en
P2093
P356
10.1038/87582
P577
2001-05-01T00:00:00Z