1kp5: Difference between revisions

Revision as of 14:36, 21 February 2008

Cyclic Green Fluorescent Protein

OverviewOverview

Crystals of cyclic green fluorescent protein (cGFP) engineered by the previously reported split intein technology [Iwai et al. (2001), J. Biol. Chem. 276, 16548-16554] were obtained and the structure was solved using molecular replacement. Although the core of the protein can unambiguously be fitted from the first to the last residue of the genuine sequence, the electron density in the region of the linker peptide is rather poor owing to the high water content of the crystals. Therefore, it is concluded that this part of the protein is highly disordered in the present structure and is very flexible. This is supported by the absence of crystal contacts in the linker-peptide region and the fact that the core of the protein exhibits a very similar conformation to that known from other GFP structures, thereby not implicating any constraints arising from the presence of the artificial linker. Nevertheless, the density is consistent with the loop being intact, as confirmed by mass spectroscopy of dissolved crystals. The present structure contains an antiparallel cGFP dimer where the dimer interface is clearly different from other crystal structures featuring two GFP molecules. This adds further support to the fact that the cylinder surface of GFP is rather versatile and can employ various polar and non-polar patches in protein-protein interactions.

About this StructureAbout this Structure

1KP5 is a Single protein structure of sequence from Aequorea victoria with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Structure of cyclized green fluorescent protein., Hofmann A, Iwai H, Hess S, Pluckthun A, Wlodawer A, Acta Crystallogr D Biol Crystallogr. 2002 Sep;58(Pt 9):1400-6. Epub 2002, Aug 23. PMID:12198295

Page seeded by OCA on Thu Feb 21 13:36:31 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1kp5.jpg|left|200px]]<br /><applet load="1kp5" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1kp5.jpg|left|200px]]<br /><applet load="1kp5" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1kp5, resolution 2.6&Aring;" />
 '''Cyclic Green Fluorescent Protein'''<br />
 ==Overview==
-Crystals of cyclic green fluorescent protein (cGFP) engineered by the, previously reported split intein technology [Iwai et al. (2001), J. Biol., Chem. 276, 16548-16554] were obtained and the structure was solved using, molecular replacement. Although the core of the protein can unambiguously, be fitted from the first to the last residue of the genuine sequence, the, electron density in the region of the linker peptide is rather poor owing, to the high water content of the crystals. Therefore, it is concluded that, this part of the protein is highly disordered in the present structure and, is very flexible. This is supported by the absence of crystal contacts in, the linker-peptide region and the fact that the core of the protein, exhibits a very similar conformation to that known from other GFP, structures, thereby not implicating any constraints arising from the, presence of the artificial linker. Nevertheless, the density is consistent, with the loop being intact, as confirmed by mass spectroscopy of dissolved, crystals. The present structure contains an antiparallel cGFP dimer where, the dimer interface is clearly different from other crystal structures, featuring two GFP molecules. This adds further support to the fact that, the cylinder surface of GFP is rather versatile and can employ various, polar and non-polar patches in protein-protein interactions.
+Crystals of cyclic green fluorescent protein (cGFP) engineered by the previously reported split intein technology [Iwai et al. (2001), J. Biol. Chem. 276, 16548-16554] were obtained and the structure was solved using molecular replacement. Although the core of the protein can unambiguously be fitted from the first to the last residue of the genuine sequence, the electron density in the region of the linker peptide is rather poor owing to the high water content of the crystals. Therefore, it is concluded that this part of the protein is highly disordered in the present structure and is very flexible. This is supported by the absence of crystal contacts in the linker-peptide region and the fact that the core of the protein exhibits a very similar conformation to that known from other GFP structures, thereby not implicating any constraints arising from the presence of the artificial linker. Nevertheless, the density is consistent with the loop being intact, as confirmed by mass spectroscopy of dissolved crystals. The present structure contains an antiparallel cGFP dimer where the dimer interface is clearly different from other crystal structures featuring two GFP molecules. This adds further support to the fact that the cylinder surface of GFP is rather versatile and can employ various polar and non-polar patches in protein-protein interactions.
 ==About this Structure==
-KP5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aequorea_victoria Aequorea victoria] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KP5 OCA].
+KP5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aequorea_victoria Aequorea victoria] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KP5 OCA].
 ==Reference==
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 [[Category: green fluorescent protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:33:07 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:36:31 2008''