PDBsum entry 1srv

Chaperone

PDB id: 1srv

Contents

Protein chain

145 a.a. *

Waters ×80

* Residue conservation analysis

References listed in PDB file

Key reference

Title

Taking mad to the extreme: ultrafast protein structure determination.

Authors

M.A.Walsh, I.Dementieva, G.Evans, R.Sanishvili, A.Joachimiak.

Ref.

Acta Crystallogr D Biol Crystallogr, 1999, 55, 1168-1173. [DOI no: 10.1107/S0907444999003698]

PubMed id

10329779

Abstract

Multiwavelength anomalous diffraction data were measured in 23 min from a 16 kDa selenomethionyl substituted protein, producing experimental phases to 2.25 A resolution. The data were collected on a mosaic 3 x 3 charge-coupled device using undulator radiation from the Structural Biology Center 19ID beamline at the Argonne National Laboratory's Advanced Photon Source. The phases were independently obtained semiautomatically by two crystallographic program suites, CCP4 and CNS. The quality and speed of this data acquisition exemplify the opportunities at third-generation synchrotron sources for high-throughput protein crystal structure determination.

Figure 3.
Figure 3 Residue-based real-space map correlation coefficient (RSCC; Brändén & Jones, 1990[Brändén, C.-I. & Jones, T. A. (1990). Nature (London), 343, 687-689.]) for the experimental and DM solvent-flattened electron-density maps for the AD of T. thermophilus chaperonin at 2.25 Å resolution.

The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (1999, 55, 1168-1173) copyright 1999.

Secondary reference #1

Title

A structural model for groel-Polypeptide recognition.

Authors

A.M.Buckle, R.Zahn, A.R.Fersht.

Ref.

Proc Natl Acad Sci U S A, 1997, 94, 3571-3575. [DOI no: 10.1073/pnas.94.8.3571]

PubMed id

9108017

Figure 2.
Fig. 2. (Top) Stereo cartoon representation of the structure of the mini-chaperone (GroEL191-376), showing the interaction between the N-terminal tag and a neighboring molecule in the crystal lattice^ (related by a crystallographic two-fold screw operation along the c axis, positioned approximately vertical and in the plane^ of the paper). The N-terminal tag (residues 1 to 7) is colored^ yellow. (Middle) Close-up of peptide-binding site interactions, in stereo. The peptide is represented by yellow bonds; neighboring residues are represented by white bonds. Hydrogen bonds are represented^ by broken white lines. Drawn with BOBSCRIPT (extensions to the^ program MOLSCRIPT; ref. 24) and RASTER3D (25). (Lower) As in Middle but showing the molecular surface of the mini-chaperone. The surface is colored according to surface curvature to highlight concave surface pockets. Convex, concave, and flat surfaces are^ colored green, grey, and white, respectively. Residues underlying the surface are labeled. Drawn with GRASP (26). All three figures show the model in approximately the same orientation.

Figure 4.
Fig. 4. (Upper) Stereoview of one heptameric ring of the GroEL tetradecamer showing the position of the N-terminal tag bound to each apical domain, near the opening to the central cavity. This model is generated by the superposition of the mini-chaperone GroEL(191-376) with each corresponding apical domain (residues 191-376) in intact GroEL (the second ring of the GroEL cylinder, generated by a two-fold^ symmetry operation, is not shown, but stacks against the underside^ of the drawn ring). GroEL subunits are colored around the ring going from blue to green. Superimposed "bound peptides" are colored^ from green to red. Drawn with RASMOL (32). (Lower) Cross-section of the model shown in Upper looking directly at the inner wall of the cavity, and showing the apical domains (cartoon with helices H8 and H9 colored cyan) from three subunits with modeled peptide^ (shown as space-filling models colored yellow, orange, and red, respectively). Drawn with MOLSCRIPT (24) and RASTER3D (25). Each of the separate peptides (residues 1 to 7) could be linked^ together by small fragments of peptides so that a longer peptide^ could bind from one contiguous site to the next.