4eab: Difference between revisions
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[[Image:4eab. | [[Image:4eab.png|left|200px]] | ||
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===X-ray crystal structure of the H141A mutant of GDP-perosamine N-acetyl transferase from Caulobacter crescentus in complex with CoA and GDP-perosamine=== | ===X-ray crystal structure of the H141A mutant of GDP-perosamine N-acetyl transferase from Caulobacter crescentus in complex with CoA and GDP-perosamine=== | ||
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The line below this paragraph, {{ABSTRACT_PUBMED_22443398}}, adds the Publication Abstract to the page | |||
(as it appears on PubMed at http://www.pubmed.gov), where 22443398 is the PubMed ID number. | |||
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{{ABSTRACT_PUBMED_22443398}} | |||
==About this Structure== | ==About this Structure== | ||
[[4eab]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Caulobacter_vibrioides Caulobacter vibrioides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EAB OCA]. | [[4eab]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Caulobacter_vibrioides Caulobacter vibrioides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EAB OCA]. | ||
==Reference== | |||
<ref group="xtra">PMID:022443398</ref><references group="xtra"/> | |||
[[Category: Caulobacter vibrioides]] | [[Category: Caulobacter vibrioides]] | ||
[[Category: Cleland, W W.]] | [[Category: Cleland, W W.]] | ||
Revision as of 06:16, 11 April 2012
X-ray crystal structure of the H141A mutant of GDP-perosamine N-acetyl transferase from Caulobacter crescentus in complex with CoA and GDP-perosamine
Template:ABSTRACT PUBMED 22443398
About this Structure
4eab is a 1 chain structure with sequence from Caulobacter vibrioides. Full crystallographic information is available from OCA.
Reference
- Thoden JB, Reinhardt LA, Cook PD, Menden P, Cleland WW, Holden HM. The Catalytic Mechanism of Perosamine N-Acetyltransferase Revealed by High Resolution X-ray Crystallographic Studies and Kinetic Analyses. Biochemistry. 2012 Mar 23. PMID:22443398 doi:10.1021/bi300197h
