2PF1

STRUCTURE OF BOVINE PROTHROMBIN FRAGMENT 1 REFINED AT 2.25 ANGSTROMS RESOLUTION

Summary for 2PF1

• Entry DOI: 10.2210/pdb2pf1/pdb
• Descriptor: PROTHROMBIN FRAGMENT 1 (2 entities in total)
• Functional Keywords: hydrolase(serine proteinase)
• Biological source: Bos taurus (cattle)
• Cellular location: Secreted, extracellular space: P00735
• Total number of polymer chains: 1
• Total formula weight: 18024.67

Authors

Seshadri, T.P.,Tulinsky, A.,Skrzypczak-Jankun, E.,Park, C.H. (deposition date: 1992-09-17, release date: 1994-01-31, Last modification date: 2025-03-26)

Primary citation

Seshadri, T.P.,Tulinsky, A.,Skrzypczak-Jankun, E.,Park, C.H.
Structure of bovine prothrombin fragment 1 refined at 2.25 A resolution.
J.Mol.Biol., 220:481-494, 1991

PubMed Abstract: The structure of bovine prothrombin fragment 1 has been refined at 2.25 A resolution using high resolution measurements made with the synchrotron beam at CHESS. The synchrotron data were collected photographically by oscillation methods (R-merge = 0.08). These were combined with lower order diffractometer data for refinement purposes. The structure was refined using restrained least-squares methods with the program PROLSQ to a crystallographic R-value of 0.175. The structure includes 105 water molecules with occupancies of greater than 0.6. The first 35 residues (Ala1-Leu35) of the N-terminal gamma-carboxy glutamic acid-domain (Ala1-Cys48) of fragment 1 are disordered as are two carbohydrate chains of Mr approximately 5000; the latter two combine to render 40% of the structure disordered. The folding of the kringle of fragment 1 is related to the close intramolecular contact between the inner loop disulfide groups. Half of the conserved sequence of the kringle forms an inner core surrounding these disulfide groups. The remainder of the sequence conservation is associated with the many turns of the main chain. The Pro95 residue of the kringle has a cis conformation and Tyr74 is ordered in fragment 1, although nuclear magnetic resonance studies indicate that the comparable residue of plasminogen kringle 4 has two positions. Surface accessibility calculations indicate that none of the disulfide groups of fragment 1 is accessible to solvent.

PubMed: 1856869
DOI: 10.1016/0022-2836(91)90025-2

Experimental method

X-RAY DIFFRACTION (2.8 Å)