1gsi: Difference between revisions
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[[Category: transferase (atp:tmp phosphotransferase)]] | [[Category: transferase (atp:tmp phosphotransferase)]] | ||
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Revision as of 16:13, 30 October 2007
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CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS THYMIDYLATE KINASE COMPLEXED WITH THYMIDINE MONOPHOSPHATE (TMP)
OverviewOverview
Caged compounds in combination with protein crystallography represent a, valuable tool in studies of enzyme reaction intermediates. To date, photochemical triggering of reactions has been performed close to room, temperature. Synchronous reaction initiation has only been achieved with, enzymes of relatively slow turnover (<0.1 s(-1)) and caged compounds of, high quantum yield. Here X-ray crystallography and microspectrophotometry, were used to provide evidence that (nitrophenyl)ethyl (NPE) ester bonds, can be photolyzed by UV light at cryotemperatures. NPE-caged ATP in, flash-cooled crystals of Mycobacterium tuberculosis thymidylate kinase was, photolyzed successfully at 100-150 K as assessed by the structural, observation of ATP-dependent enzymatic conversion of TMP to TDP after, ... [(full description)]
About this StructureAbout this Structure
1GSI is a [Single protein] structure of sequence from [Mycobacterium tuberculosis] with MG, SO4, ACT and TMP as [ligands]. Active as [dTMP kinase], with EC number [2.7.4.9]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Cryophotolysis of caged compounds: a technique for trapping intermediate states in protein crystals., Ursby T, Weik M, Fioravanti E, Delarue M, Goeldner M, Bourgeois D, Acta Crystallogr D Biol Crystallogr. 2002 Apr;58(Pt 4):607-14. Epub 2002, Mar 22. PMID:11914484
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