1za2

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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==
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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].
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[[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==
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<ref group="xtra">PMID:15951418</ref><references group="xtra"/>
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<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]]
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[[Category: X-ray crystallography]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 08:17:25 2009''
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Revision as of 10:10, 16 November 2011

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

  • 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
  • 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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