2a0f: Difference between revisions

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==About this Structure==
==About this Structure==
2A0F is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A0F OCA].  
2A0F is a 4 chains structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A0F OCA].  


==Reference==
==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/16120448 16120448]
<ref group="xtra">PMID:16120448</ref><references group="xtra"/>
[[Category: Aspartate carbamoyltransferase]]
[[Category: Aspartate carbamoyltransferase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Protein complex]]
[[Category: Cardia, J P.]]
[[Category: Cardia, J P.]]
[[Category: Dusinberre, K J.]]
[[Category: Dusinberre, K J.]]
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[[Category: Homotropic cooperativity]]
[[Category: Homotropic cooperativity]]


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Revision as of 22:38, 17 February 2009

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 4 chains structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

[xtra 1]

  1. Stieglitz KA, Dusinberre KJ, Cardia JP, Tsuruta H, Kantrowitz ER. Structure of the E.coli aspartate transcarbamoylase trapped in the middle of the catalytic cycle. J Mol Biol. 2005 Sep 16;352(2):478-86. PMID:16120448 doi:10.1016/j.jmb.2005.07.046

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