PDBsum entry 1bff

Growth factor

PDB id: 1bff

Contents

Protein chain

129 a.a. *

Ligands

PO4

BME

Waters ×67

* Residue conservation analysis

PDB id:

1bff

Name:

Growth factor

Title:

The 154 amino acid form of human basic fibroblast growth factor

Structure:

Basic fibroblast growth factor. Chain: a. Synonym: bfgf. Engineered: yes

Source:

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

Resolution:

2.00Å R-factor: 0.190

Authors:

J.S.Kastrup,E.S.Eriksson

Key ref:

J.S.Kastrup et al. (1997). X-ray structure of the 154-amino-acid form of recombinant human basic fibroblast growth factor. comparison with the truncated 146-amino-acid form. Acta Crystallogr D Biol Crystallogr, 53, 160-168. PubMed id: 15299950 DOI: 10.1107/S0907444996012711

Date:

06-Dec-96 Release date: 16-Jun-97

Protein chain

P09038  (FGF2_HUMAN) -  Fibroblast growth factor 2 from Homo sapiens

Seq: 288 a.a.

Struc: 129 a.a.

DOI no: 10.1107/S0907444996012711

Acta Crystallogr D Biol Crystallogr 53:160-168 (1997)

PubMed id: 15299950

X-ray structure of the 154-amino-acid form of recombinant human basic fibroblast growth factor. comparison with the truncated 146-amino-acid form.

J.S.Kastrup, E.S.Eriksson, H.Dalbøge, H.Flodgaard.

ABSTRACT

The crystal structure of the 154-amino-acid form of human basic fibroblast growth factor (hbFGF154), probably representing the intact form of hbFGF as deduced from the open reading frame of hbFGF cDNA, was determined by X-ray crystallography and refined to a crystallographic residual of 19.0% for all data between 20.0 and 2.0 A resolution. Crystals were obtained from recombinant hbFGF154 expressed in E. coli. hbFGF154 has the same overall structure as the N-terminus truncated 146-amino-acid form. The structure has a Kunitz-type fold and is built of 12 beta-strands of which six antiparallel strands form a beta-sheet barrel. In the structure it was possible to locate two additional residues at the N terminus and the last three C-terminal amino-acid residues, which seem to be disordered in all but one of the reported structures of the truncated form of hbFGF. The C-terminal amino-acid residues are part of the last beta-strand through the formation of a hydrogen bond between the main-chain amide group of Ala152 and the carbonyl O atom of Pro28. An apparent phosphate ion is bound within the basic region on the surface of the molecule and has as ligands the side chains of Asn35, Arg128 and Lys133 and two water molecules. A slightly different hydrogen-bonding pattern to the phosphate ion is observed as compared with the sulfate ions in the truncated forms [Eriksson, Cousens & Matthews (1993). Protein Sci. 2, 1274-1284; Zhang, Cousens, Barr & Sprang (1991). Proc. Natl Acad. Sci. USA, 88, 3446-3450]. One molecule of beta-mercaptoethanol forms a disulfide bridge to Cys77.

Selected figure(s)

Figure 1.
Fig. 1. Schematic picture of the fl-trefoil fold of hbFGF 154 (a) viewed along an axis of approximate threefold symmetry and (b) rotated 90 °. Arrows represent/]-strands and rattlers coils. (ill: 28-34, f12: 37-43, /33: 46-51, /34: 60-67, /35: 69-76, /36: 79-85, /37: 88-93, /38: 101-107,/39: 110-117,/310: 122-127,/311: 130-133, and/312: 146-152.)

Figure 5.
Fig. 5. (a) Difference Fourier map (OMIT map) at the phosphate- binding site after rigid-body refinements without any ion included. Contours drawn at a level of 3a where a is the root- mean-square density throughout the unit cell. (b) The phosphate- binding site in hbFGF 154 showing the pattern of hydrogen bonds (less than 3.0A, dotted lines) to the phosphate ion and the corre- sponding distances. 03 also forms hydrogen bonds to the side-chain N ~ atom of Arg 128 (3.1 ~,) and to water 181 (3.1A). (c) A super- imposition of the phosphate-bind- ing site of hbFGF154 (red), the corresponding sulfate-binding site of wt-Eriksson (green) and wt- Zhang (blue), and wt-Ago (black), mt-Ago (yellow), and mt-Zhu (cyan).

The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (1997, 53, 160-168) copyright 1997.

Figures were selected by an automated process.