2roq: Difference between revisions

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{{Seed}}
[[Image:2roq.png|left|200px]]
[[Image:2roq.png|left|200px]]


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{{STRUCTURE_2roq|  PDB=2roq  |  SCENE=  }}  
{{STRUCTURE_2roq|  PDB=2roq  |  SCENE=  }}  


===Solution Structure of the thiolation-thioesterase di-domain of enterobactin synthetase component F===
===Solution Structure of the thiolation-thioesterase di-domain of enterobactin synthetase component F===


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The line below this paragraph, {{ABSTRACT_PUBMED_18704088}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_18704088}}
{{ABSTRACT_PUBMED_18704088}}


==About this Structure==
==About this Structure==
2ROQ is a 1 chain structure of 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=2ROQ OCA].  
[[2roq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ROQ OCA].  


==Reference==
==Reference==
<ref group="xtra">PMID:18704088</ref><references group="xtra"/>
<ref group="xtra">PMID:018704088</ref><references group="xtra"/>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Arthanari, H.]]
[[Category: Arthanari, H.]]
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[[Category: Transferase]]
[[Category: Transferase]]
[[Category: Transport]]
[[Category: Transport]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr  8 20:11:44 2009''

Revision as of 19:29, 7 January 2013

File:2roq.png

Template:STRUCTURE 2roq

Solution Structure of the thiolation-thioesterase di-domain of enterobactin synthetase component F

Template:ABSTRACT PUBMED 18704088

About this Structure

2roq is a 1 chain structure with sequence from Escherichia coli. Full experimental information is available from OCA.

Reference

  1. Frueh DP, Arthanari H, Koglin A, Vosburg DA, Bennett AE, Walsh CT, Wagner G. Dynamic thiolation-thioesterase structure of a non-ribosomal peptide synthetase. Nature. 2008 Aug 14;454(7206):903-6. PMID:18704088 doi:10.1038/nature07162

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