2m3x | pdb_00002m3x

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Solution structure of Ph1500: a homohexameric protein centered on a 12-bladed beta-propeller

spinqualitylabelsall models 2m3x, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2m3x is a 6 chain structure with sequence from Pyrococcus horikoshii. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 2jv2 Gene: PH1500 (Pyrococcus horikoshii) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Warning: this is a large structure, and loading might take a long time or not happen at all. Publication Abstract from PubMed Ph1500 is a homohexameric, two-domain protein of unknown function from the hyperthermophilic archaeon Pyrococcus horikoshii. The C-terminal hexamerization domain (Ph1500C) is of particular interest, as it lacks sequence homology to proteins of known structure. However, it resisted crystallization for X-ray analysis, and proteins of this size (49 kDa) present a considerable challenge to NMR structure determination in solution. We solved the high-resolution structure of Ph1500C, exploiting the hyperthermophilic nature of the protein to minimize unfavorable relaxation properties by high-temperature measurement. Thus, the side chain assignment (97%) and structure determination became possible at full proton density. To our knowledge, Ph1500C is the largest protein for which this has been achieved. To minimize detrimental fast water exchange of amide protons at increased temperature, we employed a strategy where the temperature was optimized separately for backbone and side chain experiments. Optimized measurement temperature gives access to the solution structure of a 49 kDa homohexameric beta-propeller.,Varnay I, Truffault V, Djuranovic S, Ursinus A, Coles M, Kessler H J Am Chem Soc. 2010 Nov 10;132(44):15692-8. doi: 10.1021/ja1064608. PMID:20961124 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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