1za2: Difference between revisions

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{{Seed}}
[[Image:1za2.png|left|200px]]
[[Image:1za2.png|left|200px]]


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==About this Structure==
==About this Structure==
1ZA2 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=1ZA2 OCA].  
[[1za2]] is a 4 chain structure with sequence 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=1ZA2 OCA].  


==Reference==
==Reference==
<ref group="xtra">PMID:15951418</ref><references group="xtra"/>
<ref group="xtra">PMID:015951418</ref><ref group="xtra">PMID:016120448</ref><references group="xtra"/>
[[Category: Aspartate carbamoyltransferase]]
[[Category: Aspartate carbamoyltransferase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Cooperativity]]
[[Category: Cooperativity]]
[[Category: Ordered substrate binding]]
[[Category: Ordered substrate binding]]
[[Category: X-ray crystallography]]
[[Category: Transferase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 08:17:25 2009''

Revision as of 10:10, 16 November 2011

File:1za2.png

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 4 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

  1. Wang J, Stieglitz KA, Cardia JP, Kantrowitz ER. Structural basis for ordered substrate binding and cooperativity in aspartate transcarbamoylase. Proc Natl Acad Sci U S A. 2005 Jun 21;102(25):8881-6. Epub 2005 Jun 10. PMID:15951418
  2. 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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