1za1: Difference between revisions

Revision as of 04:57, 28 July 2008

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File:1za1.png

Template:STRUCTURE 1za1

Structure of wild-type E. coli Aspartate Transcarbamoylase in the presence of CTP at 2.20 A resolutionStructure of wild-type E. coli Aspartate Transcarbamoylase in the presence of CTP at 2.20 A resolution

Template:ABSTRACT PUBMED 15951418

About this StructureAbout this Structure

1ZA1 is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for ordered substrate binding and cooperativity in aspartate transcarbamoylase., Wang J, Stieglitz KA, Cardia JP, Kantrowitz ER, Proc Natl Acad Sci U S A. 2005 Jun 21;102(25):8881-6. Epub 2005 Jun 10. PMID:15951418

Page seeded by OCA on Mon Jul 28 04:57:54 2008

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

OCA

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-'''Structure of wild-type E. coli Aspartate Transcarbamoylase in the presence of CTP at 2.20 A resolution'''
+===Structure of wild-type E. coli Aspartate Transcarbamoylase in the presence of CTP at 2.20 A resolution===
-==Overview==
+<!--
-X-ray structures of aspartate transcarbamoylase in the absence and presence of the first substrate carbamoyl phosphate are reported. These two structures in conjunction with in silico docking experiments provide snapshots of critical events in the function of the enzyme. The ordered substrate binding, observed experimentally, can now be structurally explained by a conformational change induced upon the binding of carbamoyl phosphate. This induced fit dramatically alters the electrostatics of the active site, creating a binding pocket for aspartate. Upon aspartate binding, a further change in electrostatics causes a second induced fit, the domain closure. This domain closure acts as a clamp that both facilitates catalysis by approximation and also initiates the global conformational change that manifests homotropic cooperativity.
+The line below this paragraph, {{ABSTRACT_PUBMED_15951418}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_15951418}}
 ==About this Structure==
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 [[Category: Ordered substrate binding]]
 [[Category: X-ray crystallography]]
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