3bwd
Crystal structure of the plant Rho protein ROP5Crystal structure of the plant Rho protein ROP5
Structural highlights
Function[RAC6_ARATH] May be involved in cell polarity control during the actin-dependent tip growth of pollen tubes.[1] [2] Inactive GDP-bound Rho GTPases reside in the cytosol, are found in a complex with Rho GDP-dissociation inhibitors (Rho GDIs), and are released from the GDI protein in order to translocate to membranes upon activation (By similarity).[3] [4] Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe small G protein ROP5 from the model plant Arabidopsis thaliana was purified and crystallized using the hanging-drop vapour-diffusion method. ROP5 crystals were obtained using PEG 3000 as precipitant and belong to space group P2(1). A data set was collected to 1.53 A resolution using synchrotron radiation at 100 K. A clear molecular-replacement solution was found using ROP4-GDP of the ROP4-GDP-PRONE8 complex as the search model. Purification, crystallization and preliminary X-ray diffraction analysis of the plant Rho protein ROP5.,Thomas C, Berken A Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Dec 1;63(Pt, 12):1070-2. Epub 2007 Nov 30. PMID:18084097[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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