1uis
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(New page: 200px<br /><applet load="1uis" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uis, resolution 2.0Å" /> '''The 2.0 crystal struc...)
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Revision as of 02:02, 21 November 2007
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The 2.0 crystal structure of eqFP611, a far-red fluorescent protein from the sea anemone Entacmaea quadricolor
Overview
We have crystallized and subsequently determined to 2.0-A resolution the, crystal structure of eqFP611, a far red fluorescent protein from the sea, anemone Entacmaea quadricolor. The structure of the protomer, which adopts, a beta-can topology, is similar to that of the related monomeric green, fluorescent protein (GFP). The quaternary structure of eqFP611, a tetramer, exhibiting 222 symmetry, is similar to that observed for the more closely, related red fluorescent protein DsRed and the chromoprotein Rtms5. The, unique chromophore sequence (Met63-Tyr64-Gly65) of eqFP611, adopts a, coplanar and trans conformation within the interior of the beta-can fold., Accordingly, the eqFP611 chromophore adopts a significantly different, conformation in comparison to the chromophore conformation observed in, GFP, DsRed, and Rtms5. The coplanar chromophore conformation and its, immediate environment provide a structural basis for the far red, highly, fluorescent nature of eqFP611. The eqFP611 structure extends our knowledge, on the range of conformations a chromophore can adopt within closely, related members of the green fluorescent protein family.
About this Structure
1UIS is a Single protein structure of sequence from Entacmaea quadricolor with CA and ACY as ligands. Full crystallographic information is available from OCA.
Reference
The 2.0-A crystal structure of eqFP611, a far red fluorescent protein from the sea anemone Entacmaea quadricolor., Petersen J, Wilmann PG, Beddoe T, Oakley AJ, Devenish RJ, Prescott M, Rossjohn J, J Biol Chem. 2003 Nov 7;278(45):44626-31. Epub 2003 Aug 8. PMID:12909624
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