1za2

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[[Image:1za2.gif|left|200px]]
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{{STRUCTURE_1za2| PDB=1za2 | SCENE= }}
{{STRUCTURE_1za2| PDB=1za2 | SCENE= }}
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'''Structure of wild-type E. coli Aspartate Transcarbamoylase in the presence of CTP, carbamoyl phosphate at 2.50 A resolution'''
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===Structure of wild-type E. coli Aspartate Transcarbamoylase in the presence of CTP, carbamoyl phosphate at 2.50 A resolution===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15951418 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15951418}}
==About this Structure==
==About this Structure==
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[[Category: Ordered substrate binding]]
[[Category: Ordered substrate binding]]
[[Category: X-ray crystallography]]
[[Category: X-ray crystallography]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:22:27 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:38:17 2008''

Revision as of 11:38, 29 July 2008

Template:STRUCTURE 1za2

Structure of wild-type E. coli Aspartate Transcarbamoylase in the presence of CTP, carbamoyl phosphate at 2.50 A resolution

Template:ABSTRACT PUBMED 15951418

About this Structure

1ZA2 is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

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

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