PDBsum entry 1q04

Hormone/growth factor

PDB id: 1q04

Contents

Protein chains

141 a.a. *

Ligands

FMT ×4

Waters ×194

* Residue conservation analysis

PDB id:

1q04

Name:

Hormone/growth factor

Title:

Crystal structure of fgf-1, s50e/v51n

Structure:

Heparin-binding growth factor 1. Chain: a, b. Synonym: acidic fibroblast growth factor. Fgf-1. Hbgf-1. Afgf. Beta- endothelial cell growth factor. Ecgf-beta. Fibroblast growth factor 1. Engineered: yes. Mutation: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.80Å R-factor: 0.185 R-free: 0.214

Authors:

J.Kim,M.Blaber

Key ref:

J.Kim et al. (2005). Sequence swapping does not result in conformation swapping for the beta4/beta5 and beta8/beta9 beta-hairpin turns in human acidic fibroblast growth factor. Protein Sci, 14, 351-359. PubMed id: 15632285 DOI: 10.1110/ps.041094205

Date:

15-Jul-03 Release date: 27-Jul-04

Protein chains

P05230  (FGF1_HUMAN) -  Fibroblast growth factor 1 from Homo sapiens

Seq: 155 a.a.

Struc: 141 a.a.*

* PDB and UniProt seqs differ at 6 residue positions (black crosses)

DOI no: 10.1110/ps.041094205

Protein Sci 14:351-359 (2005)

PubMed id: 15632285

Sequence swapping does not result in conformation swapping for the beta4/beta5 and beta8/beta9 beta-hairpin turns in human acidic fibroblast growth factor.

J.Kim, J.Lee, S.R.Brych, T.M.Logan, M.Blaber.

ABSTRACT

The beta-turn is the most common type of nonrepetitive structure in globular proteins, comprising ~25% of all residues; however, a detailed understanding of effects of specific residues upon beta-turn stability and conformation is lacking. Human acidic fibroblast growth factor (FGF-1) is a member of the beta-trefoil superfold and contains a total of five beta-hairpin structures (antiparallel beta-sheets connected by a reverse turn). beta-Turns related by the characteristic threefold structural symmetry of this superfold exhibit different primary structures, and in some cases, different secondary structures. As such, they represent a useful system with which to study the role that turn sequences play in determining structure, stability, and folding of the protein. Two turns related by the threefold structural symmetry, the beta4/beta5 and beta8/beta9 turns, were subjected to both sequence-swapping and poly-glycine substitution mutations, and the effects upon stability, folding, and structure were investigated. In the wild-type protein these turns are of identical length, but exhibit different conformations. These conformations were observed to be retained during sequence-swapping and glycine substitution mutagenesis. The results indicate that the beta-turn structure at these positions is not determined by the turn sequence. Structural analysis suggests that residues flanking the turn are a primary structural determinant of the conformation within the turn.

Selected figure(s)

Figure 4.
Figure 4. Relaxed stereo diagram illustrating an overlay of the 4/ 5 turn regions for WT* (CPK coloring), V51N (red), S50G/V51G (magenta), and S50E/V51N (green) mutants. None of the sequence substitution, or polyglycine substitutions, within this turn affected the structure of the turn.

Figure 5.
Figure 5. Relaxed stereo diagram of a close-up of an overlay of the 4/ 5 (light gray) and 8/ 9 (dark gray) turns showing the local side chain interactions.

The above figures are reprinted by permission from the Protein Society: Protein Sci (2005, 14, 351-359) copyright 2005.

Figures were selected by the author.