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1za1
From Proteopedia
(Difference between revisions)
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[[Image:1za1.png|left|200px]] | [[Image:1za1.png|left|200px]] | ||
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{{STRUCTURE_1za1| PDB=1za1 | SCENE= }} | {{STRUCTURE_1za1| PDB=1za1 | SCENE= }} | ||
===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=== | ||
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{{ABSTRACT_PUBMED_15951418}} | {{ABSTRACT_PUBMED_15951418}} | ||
==About this Structure== | ==About this Structure== | ||
| - | + | [[1za1]] 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=1ZA1 OCA]. | |
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:015951418</ref><ref group="xtra">PMID:020681545</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: | + | [[Category: Transferase]] |
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Revision as of 17:20, 5 January 2013
Structure of wild-type E. coli Aspartate Transcarbamoylase in the presence of CTP at 2.20 A resolution
Template:ABSTRACT PUBMED 15951418
About this Structure
1za1 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
- Mendes KR, Kantrowitz ER. A cooperative Escherichia coli aspartate transcarbamoylase without regulatory subunits . Biochemistry. 2010 Sep 7;49(35):7694-703. PMID:20681545 doi:10.1021/bi1010333
