2a0f: Difference between revisions

Revision as of 05:47, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2a0f.png

Template:STRUCTURE 2a0f

Structure of D236A mutant E. coli Aspartate Transcarbamoylase in presence of Phosphonoacetamide at 2.90 A resolutionStructure of D236A mutant E. coli Aspartate Transcarbamoylase in presence of Phosphonoacetamide at 2.90 A resolution

Template:ABSTRACT PUBMED 16120448

About this StructureAbout this Structure

2A0F is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Structure of the E.coli aspartate transcarbamoylase trapped in the middle of the catalytic cycle., Stieglitz KA, Dusinberre KJ, Cardia JP, Tsuruta H, Kantrowitz ER, J Mol Biol. 2005 Sep 16;352(2):478-86. PMID:16120448

Page seeded by OCA on Tue Jul 29 05:47:11 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 {{STRUCTURE_2a0f|  PDB=2a0f  |  SCENE=  }}
-'''Structure of D236A mutant E. coli Aspartate Transcarbamoylase in presence of Phosphonoacetamide at 2.90 A resolution'''
+===Structure of D236A mutant E. coli Aspartate Transcarbamoylase in presence of Phosphonoacetamide at 2.90 A resolution===
-==Overview==
+<!--
-Snapshots of the catalytic cycle of the allosteric enzyme aspartate transcarbamoylase have been obtained via X-ray crystallography. The enzyme in the high-activity high-affinity R state contains two catalytic chains in the asymmetric unit that are different. The active site in one chain is empty, while the active site in the other chain contains an analog of the first substrate to bind in the ordered mechanism of the reaction. Small angle X-ray scattering shows that once the enzyme is converted to the R state, by substrate binding, the enzyme remains in the R state until substrates are exhausted. Thus, this structure represents the active form of the enzyme trapped at two different stages in the catalytic cycle, before the substrates bind (or after the products are released), and after the first substrate binds. Opening and closing of the catalytic chain domains explains how the catalytic cycle occurs while the enzyme remains globally in the R-quaternary structure.
+The line below this paragraph, {{ABSTRACT_PUBMED_16120448}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_16120448}}
 ==About this Structure==
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 [[Category: Catalytic cycle]]
 [[Category: Homotropic cooperativity]]
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