PDBsum entry 1oa6

Hydrolase inhibitor

PDB id: 1oa6

Contents

Protein chain

58 a.a. *

Waters ×12

* Residue conservation analysis

PDB id:

1oa6

Name:

Hydrolase inhibitor

Title:

The solution structure of bovine pancreatic trypsin inhibitor at high pressure

Structure:

Pancreatic trypsin inhibitor. Chain: 5. Synonym: bpti, aprotinin, trasylol, basic protease inhibitor

Source:

Bos taurus. Bovine. Organism_taxid: 9913. Organ: pancreas

NMR struc:

3 models

Authors:

M.P.Williamson,K.Akasaka,M.Refaee

Key ref:

M.P.Williamson et al. (2003). The solution structure of bovine pancreatic trypsin inhibitor at high pressure. Protein Sci, 12, 1971-1979. PubMed id: 12930996 DOI: 10.1110/ps.0242103

Date:

02-Jan-03 Release date: 28-Aug-03

Protein chain

P00974  (BPT1_BOVIN) -  Pancreatic trypsin inhibitor from Bos taurus

Seq: 100 a.a.

Struc: 58 a.a.

DOI no: 10.1110/ps.0242103

Protein Sci 12:1971-1979 (2003)

PubMed id: 12930996

The solution structure of bovine pancreatic trypsin inhibitor at high pressure.

M.P.Williamson, K.Akasaka, M.Refaee.

ABSTRACT

The solution structure of bovine pancreatic trypsin inhibitor (BPTI) at a pressure of 2 kbar is presented. The structure was calculated as a change from an energy-minimized low-pressure structure, using (1)H chemical shifts as restraints. The structure has changed by 0.24 A RMS, and has almost unchanged volume. The largest changes as a result of pressure are in the loop 10-16, which contains the active site of BPTI, and residues 38-42, which are adjacent to buried water molecules. Hydrogen bonds are compressed by 0.029 +/- 0.117 A, with the longer hydrogen bonds, including those to internal buried water molecules, being compressed more. The hydrophobic core is also compressed, largely from reduction of packing defects. The parts of the structure that have the greatest change are close to buried water molecules, thus highlighting the importance of water molecules as the nucleation sites for volume fluctuation of proteins in native conditions.

Selected figure(s)

Figure 1.
Figure 1. Radial distribution functions for low- and high-pressure BPTI structures. The family 8 results are shown as an illustration. Distances were calculated between all pairs of atoms (including hydrogens) and placed into 0.1 Å bins. The distributions were weighted by dividing the number in each bin by the square of the radius. (A) The functions for the low-pressure structure (solid line) and the high-pressure structure (dashed line). (B) The difference (high - low), such that a positive peak at any distance means that there are more atom pairs at this distance in the high-pressure structure than there are in the low-pressure structure.

Figure 8.
Figure 8. Relative locations of Cys51 and Phe45 in low- and high-pressure structures. The two structures were superimposed on the ring atoms of Phe45.

The above figures are reprinted by permission from the Protein Society: Protein Sci (2003, 12, 1971-1979) copyright 2003.

Figures were selected by an automated process.