2f9i: Difference between revisions

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==About this Structure==
==About this Structure==
2F9I is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F9I OCA].  
2F9I is a 4 chains structure of sequences from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F9I OCA].  


==Reference==
==Reference==
The structure of the carboxyltransferase component of acetyl-coA carboxylase reveals a zinc-binding motif unique to the bacterial enzyme., Bilder P, Lightle S, Bainbridge G, Ohren J, Finzel B, Sun F, Holley S, Al-Kassim L, Spessard C, Melnick M, Newcomer M, Waldrop GL, Biochemistry. 2006 Feb 14;45(6):1712-22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16460018 16460018]
<ref group="xtra">PMID:16460018</ref><references group="xtra"/>
[[Category: Protein complex]]
[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
[[Category: Bilder, P W.]]
[[Category: Bilder, P W.]]
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[[Category: Zinc ribbon]]
[[Category: Zinc ribbon]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:39:53 2008''
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Revision as of 21:43, 17 February 2009

File:2f9i.png

Template:STRUCTURE 2f9i

Crystal Structure of the carboxyltransferase subunit of ACC from Staphylococcus aureusCrystal Structure of the carboxyltransferase subunit of ACC from Staphylococcus aureus

Template:ABSTRACT PUBMED 16460018

About this StructureAbout this Structure

2F9I is a 4 chains structure of sequences from Staphylococcus aureus. Full crystallographic information is available from OCA.

ReferenceReference

[xtra 1]

  1. Bilder P, Lightle S, Bainbridge G, Ohren J, Finzel B, Sun F, Holley S, Al-Kassim L, Spessard C, Melnick M, Newcomer M, Waldrop GL. The structure of the carboxyltransferase component of acetyl-coA carboxylase reveals a zinc-binding motif unique to the bacterial enzyme. Biochemistry. 2006 Feb 14;45(6):1712-22. PMID:16460018 doi:10.1021/bi0520479

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