PDBsum entry: 1jkw

Cell division

PDB id: 1jkw

Contents

Protein chain

277 a.a. *

Waters ×51

* Residue conservation analysis

PDB id:

1jkw

Name:

Cell division

Title:

Structure of cyclin mcs2

Structure:

Cyclin h. Chain: a. Synonym: rcyclin h (recombinant). Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: human cyclin h. Expressed in: escherichia coli. Expression_system_taxid: 562. Other_details: his-tag removed by thrombin digestion

Biol. unit:

Dimer (from PQS)

Resolution:

2.60Å R-factor: 0.222 R-free: 0.272

Authors:

G.Andersen,A.Poterszman,D.Moras,J.C.Thierry

Key ref:

G.Andersen et al. (1996). The crystal structure of human cyclin H. FEBS Lett, 397, 65-69. PubMed id: 8941715 DOI: 10.1016/S0014-5793(96)01143-X

Date:

11-Oct-96 Release date: 11-Jan-97

Protein chain

P51946  (CCNH_HUMAN) -  Cyclin-H

Seq: 323 a.a.

Struc: 277 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 

• Cellular component: nucleus (5 terms)
• Biological process: viral reproduction (28 terms)
• Biochemical function: protein binding (6 terms)

DOI no: 10.1016/S0014-5793(96)01143-X

FEBS Lett 397:65-69 (1996)

PubMed id: 8941715

The crystal structure of human cyclin H.

G.Andersen, A.Poterszman, J.M.Egly, D.Moras, J.C.Thierry.

ABSTRACT

The crystal structure of human cyclin H has been solved at 2.6 A resolution by the MIR method and refined to an R-factor of 23.1%. The core of the molecule consists of two helical repeats adopting the canonical cyclin fold already observed in the structures of cyclin A [Brown et al. (1995) Structure 3, 1235-1247; Jeffrey et al. (1995) Nature 376, 313-320; Russo et al. (1996) Nature and TFIIB [Nikoilov et al. (1995) Nature 377, 119-128]. The N-terminal and C-terminal residues form a new domain built on two long helices interacting essentially with the first repeat of the molecule.

Selected figure(s)

Figure 1.
Fig. 1. Stereo view of the experimental 2Fo-F~ electron density map contoured at 1.7cJ after the final refinement of the cyclin H model at 2.6 A resolution. This egin of the first domain shows a cluster of hydrophobic amino acids, rich in aromatic residues, located close to the entre of helix H3, characteristic of the cyclin box.

Figure 2.
Fig. 2. The fold of human cyclin H. (A) Schematic diagram of human cyclin H using the program SETOR [32]. The secondary structures, he- lices represented as cylinders and random coil stretches of the protein, were using the program DSSP [3]. The first two compact do- mains (blue) share the common cyclin fold already observed in the structure of cyclin A [1,2]. They are built of five helices identified as H1 to H5 for the first repeat and HI' to H5' the second. The long helix H5 kinks at Gu 145 into two helices, H5~ and H5[~. HN (magenta) an HC (pink) designate the N-terminal and C-terminal helices which form a third domain characteristic of cyclin H. The view suggests the exist- ence of a pseudo-two fold axis superposing the two helical domains. (B) Stereo view of the molecule using the same orientation with the num- bering of the amino acids.

The above figures are reprinted by permission from the Federation of European Biochemical Societies: FEBS Lett (1996, 397, 65-69) copyright 1996.

Figures were selected by an automated process.