3eon: Difference between revisions
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===2.55A crystal structure of native glutaryl-coa dehydrogenase from Burkholderia pseudomallei in complex with a small molecule=== | ===2.55A crystal structure of native glutaryl-coa dehydrogenase from Burkholderia pseudomallei in complex with a small molecule=== | ||
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==About this Structure== | ==About this Structure== | ||
[[3eon]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Burkholderia_pseudomallei Burkholderia pseudomallei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EON OCA]. | |||
==Reference== | |||
<ref group="xtra">PMID:021904051</ref><ref group="xtra">PMID:019388054</ref><references group="xtra"/> | |||
[[Category: Burkholderia pseudomallei]] | [[Category: Burkholderia pseudomallei]] | ||
[[Category: Glutaryl-CoA dehydrogenase]] | [[Category: Glutaryl-CoA dehydrogenase]] | ||
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[[Category: Seattle structural genomics center for infectious disease]] | [[Category: Seattle structural genomics center for infectious disease]] | ||
[[Category: Ssgcid]] | [[Category: Ssgcid]] | ||
Revision as of 08:07, 21 September 2011
2.55A crystal structure of native glutaryl-coa dehydrogenase from Burkholderia pseudomallei in complex with a small molecule2.55A crystal structure of native glutaryl-coa dehydrogenase from Burkholderia pseudomallei in complex with a small molecule
Template:ABSTRACT PUBMED 21904051
About this StructureAbout this Structure
3eon is a 4 chain structure with sequence from Burkholderia pseudomallei. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Begley DW, Davies DR, Hartley RC, Hewitt SN, Rychel AL, Myler PJ, Van Voorhis WC, Staker BL, Stewart LJ. Probing conformational states of glutaryl-CoA dehydrogenase by fragment screening. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Sep 1;67(Pt, 9):1060-9. Epub 2011 Aug 13. PMID:21904051 doi:10.1107/S1744309111014436
- ↑ Spraggon G, Hornsby M, Shipway A, Tully DC, Bursulaya B, Danahay H, Harris JL, Lesley SA. Active site conformational changes of prostasin provide a new mechanism of protease regulation by divalent cations. Protein Sci. 2009 May;18(5):1081-94. PMID:19388054 doi:10.1002/pro.118