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1ekx
From Proteopedia
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[[Image:1ekx.png|left|200px]] | [[Image:1ekx.png|left|200px]] | ||
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{{STRUCTURE_1ekx| PDB=1ekx | SCENE= }} | {{STRUCTURE_1ekx| PDB=1ekx | SCENE= }} | ||
===THE ISOLATED, UNREGULATED CATALYTIC TRIMER OF ASPARTATE TRANSCARBAMOYLASE COMPLEXED WITH BISUBSTRATE ANALOG PALA (N-(PHOSPHONACETYL)-L-ASPARTATE)=== | ===THE ISOLATED, UNREGULATED CATALYTIC TRIMER OF ASPARTATE TRANSCARBAMOYLASE COMPLEXED WITH BISUBSTRATE ANALOG PALA (N-(PHOSPHONACETYL)-L-ASPARTATE)=== | ||
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| - | (as it appears on PubMed at http://www.pubmed.gov), where 10805770 is the PubMed ID number. | ||
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| - | {{ABSTRACT_PUBMED_10805770}} | ||
==About this Structure== | ==About this Structure== | ||
| - | + | [[1ekx]] is a 3 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=1EKX OCA]. | |
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:010805770</ref><ref group="xtra">PMID:015731101</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: Atcase catalytic subunit]] | [[Category: Atcase catalytic subunit]] | ||
[[Category: Bisubstrate analog complex]] | [[Category: Bisubstrate analog complex]] | ||
| - | + | [[Category: Transferase]] | |
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Revision as of 14:43, 8 November 2012
THE ISOLATED, UNREGULATED CATALYTIC TRIMER OF ASPARTATE TRANSCARBAMOYLASE COMPLEXED WITH BISUBSTRATE ANALOG PALA (N-(PHOSPHONACETYL)-L-ASPARTATE)
About this Structure
1ekx is a 3 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
- Endrizzi JA, Beernink PT, Alber T, Schachman HK. Binding of bisubstrate analog promotes large structural changes in the unregulated catalytic trimer of aspartate transcarbamoylase: implications for allosteric regulation. Proc Natl Acad Sci U S A. 2000 May 9;97(10):5077-82. PMID:10805770 doi:10.1073/pnas.090087197
- Shi D, Morizono H, Yu X, Roth L, Caldovic L, Allewell NM, Malamy MH, Tuchman M. Crystal structure of N-acetylornithine transcarbamylase from Xanthomonas campestris: a novel enzyme in a new arginine biosynthetic pathway found in several eubacteria. J Biol Chem. 2005 Apr 15;280(15):14366-9. Epub 2005 Feb 24. PMID:15731101 doi:10.1074/jbc.C500005200
- 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
