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PDBsum entry 1kp5
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Luminescent protein
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PDB id
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1kp5
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Structure of cyclized green fluorescent protein.
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Authors
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A.Hofmann,
H.Iwai,
S.Hess,
A.Plückthun,
A.Wlodawer.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2002,
58,
1400-1406.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Figure 2.
Figure 2 The cGFP dimer. Molecule #1 is colored in blue and
molecule #2 in dark red. For each molecule the artificial linker
is shown in red and the chromophore as well as the preceding and
the following residues are drawn explicitly (green and yellow).
The figure was created with MOLSCRIPT/BOBSCRIPT (Kraulis,
1991[Kraulis, P. J. (1991). J. Appl. Cryst. 24, 946-950.];
Esnouf, 1999[Esnouf, R. M. (1999). Acta Cryst. D55, 938-940.])
and rendered with POVRay (Persistence of Vision Development
Team, 1999[Persistence of Vision Development Team (1999). POVRay
- The Persistence of Vision Raytracer, http://www.povray.org .]).
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Figure 4.
Figure 4 The dimer interface. The explosion figure of the dimer
interface shows molecule #1 on the left and molecule #2 on the
right. The figure was created with GRASP (Nicholls,
1992[Nicholls, A. (1992). GRASP: Graphical Representation and
Analysis of Surface Properties. Columbia University, New York,
USA.]).
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The above figures are
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2002,
58,
1400-1406)
copyright 2002.
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