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PDBsum entry 2erl

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Pheromone PDB id
2erl
Contents
Protein chain
40 a.a.
Ligands
EOH
Waters ×22

References listed in PDB file
Key reference
Title A challenging case for protein crystal structure determination: the mating pheromone er-1 from euplotes raikovi.
Authors D.H.Anderson, M.S.Weiss, D.Eisenberg.
Ref. Acta Crystallogr D Biol Crystallogr, 1996, 52, 469-480. [DOI no: 10.1107/S0907444995014235]
PubMed id 15299668
Note In the PDB file this reference is annotated as "TO BE PUBLISHED". The citation details given above were identified by an automated search of PubMed on title and author names, giving a perfect match.
Abstract
Four different phasing methods have been applied to the determination of the crystal structure of the 40 amino-acid mating pheromone of the unicellular ciliated protozoan Euplotes raikovi. The difficulties, failures and successes in attempts to solve the structure by: (1) molecular replacement, (2) direct phasing using the 'Shake and Bake' algorithm, (3) isomorphous replacement, and (4) multiple-wavelength anomalous dispersion are described. The structure was first solved by molecular replacement, and then was the first successful structure determination by 'Shake and Bake' without the direct involvement of its authors. A description of the current status of the high-resolution refinement of the structure is also given. The model is refined against 1 A resolution data to an R factor of 12.9%, and includes H atoms and discretely disordered side chains.
Figure 4.
Fig. 4. Stereoview of all the protein atoms in the model of Er-l, with the anomalous Fourier superimposed (con- toured at +3or). There are peaks only at the locations of S atoms, showing that the S atoms are correctly placed. The view is similar to that in Fig. l(a) of Weiss et al. (1995). This figure was prepared with the program FRODO (Jones, 1978).
The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (1996, 52, 469-480) copyright 1996.
Secondary reference #1
Title A cooperative model for receptor recognition and cell adhesion: evidence from the molecular packing in the 1.6-A crystal structure of the pheromone er-1 from the ciliated protozoan euplotes raikovi.
Authors M.S.Weiss, D.H.Anderson, S.Raffioni, R.A.Bradshaw, C.Ortenzi, P.Luporini, D.Eisenberg.
Ref. Proc Natl Acad Sci U S A, 1995, 92, 10172-10176. [DOI no: 10.1073/pnas.92.22.10172]
PubMed id 7479748
Full text Abstract
Secondary reference #2
Title The nmr solution structure of the pheromone er-1 from the ciliated protozoan euplotes raikovi.
Authors S.Mronga, P.Luginbühl, L.R.Brown, C.Ortenzi, P.Luporini, R.A.Bradshaw, K.Wüthrich.
Ref. Protein Sci, 1994, 3, 1527-1536. [DOI no: 10.1002/pro.5560030918]
PubMed id 7833812
Full text Abstract
Secondary reference #3
Title Crystallization of the euplotes raikovi mating pheromone er-1.
Authors D.Anderson, S.Raffioni, P.Luporini, R.A.Bradshaw, D.Eisenberg.
Ref. J Mol Biol, 1990, 216, 1-2.
PubMed id 2121998
Abstract
Secondary reference #4
Title Primary structure of the mating pheromone er-1 of the ciliate euplotes raikovi.
Authors S.Raffioni, P.Luporini, B.T.Chait, S.S.Disper, R.A.Bradshaw.
Ref. J Biol Chem, 1988, 263, 18152-18159.
PubMed id 3142868
Abstract
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