PDBsum entry 2p1b

Chaperone

PDB id: 2p1b

Contents

Protein chains

(+ 4 more) 100 a.a. *

Waters ×86

* Residue conservation analysis

PDB id:

2p1b

Name:

Chaperone

Title:

Crystal structure of human nucleophosmin-core

Structure:

Nucleophosmin. Chain: a, b, c, d, e, f, g, h, i, j. Fragment: n-terminal core. Synonym: npm, nucleolar phosphoprotein b23, numatrin, nucleolar protein no38. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

2.75Å R-factor: 0.213 R-free: 0.232

Authors:

H.H.Lee,H.S.Kim,J.Y.Kang,B.I.Lee,J.Y.Ha,H.J.Yoon,S.O.Lim,G.Jung, S.W.Suh

Key ref:

H.H.Lee et al. (2007). Crystal structure of human nucleophosmin-core reveals plasticity of the pentamer-pentamer interface. Proteins, 69, 672-678. PubMed id: 17879352 DOI: 10.1002/prot.21504

Date:

03-Mar-07 Release date: 27-Mar-07

Protein chains

P06748  (NPM_HUMAN) -  Nucleophosmin from Homo sapiens

Seq: 294 a.a.

Struc: 100 a.a.

DOI no: 10.1002/prot.21504

Proteins 69:672-678 (2007)

PubMed id: 17879352

Crystal structure of human nucleophosmin-core reveals plasticity of the pentamer-pentamer interface.

H.H.Lee, H.S.Kim, J.Y.Kang, B.I.Lee, J.Y.Ha, H.J.Yoon, S.O.Lim, G.Jung, S.W.Suh.

ABSTRACT

No abstract given.

Selected figure(s)

Figure 2.
Figure 2. Structural comparison of human NPM-core decamer with other histone chaperones. (A) Comparison of human NPM-core decamer (colored in blue) and Xenopus NO38-core decamer (orange). Bottom pentamers are superimposed to display the rotational offset. Upper and lower right views are obtained by rotating the top and bottom pentamers by 90° around a horizontal axis, respectively. The views are from the center of the decamer and the viewing direction is slightly tilted from the fivefold axis to emphasize the structural difference. (B) Superposition of bottom pentamers of human NPM-core (colored in blue), Xenopus NO38-core (orange), and Xenopus nucleoplasmin-core (green). (C) Comparison of top pentamers of human NPM-core (colored in blue), Xenopus NO38-core (orange), and Xenopus nucleoplasmin-core (green) after superposition of the bottom pentamers.

Figure 3.
Figure 3. Stereo view of the pentamer-pentamer interface and the electrostatic potential at the molecular surface. (A) Stereo view of the pentamer-pentamer interface in human NPM-core (between monomers A and F). Black dotted lines denote hydrogen bonds. Highly similar interactions are repeated five times in a decamer. (B) Pentamer-pentamer interface of Xenopus NO38-core. Black dotted lines denote hydrogen bonds, while a red ball represents a water molecule. (C) Pentamer-pentamer interface of Xenopus nucleoplasmin (Np)-core. Black dotted lines denote hydrogen bonds, while red balls represent water molecules. (D) Stereo view of the region around the ARF binding loop (residues 100-117).[31] AKDE loop, GSGP loop, and the cluster of hydrophobic core-forming residues are represented by pink, light blue, and cyan colors, respectively. (E) The electrostatic potential at the molecular surface of human NPM-core, Xenopus NO38-core, and Xenopus nucleoplasmin-core. The views are down the twofold axis.

The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2007, 69, 672-678) copyright 2007.

Figures were selected by an automated process.