7pti

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[[Image:7pti.gif|left|200px]]
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{{Structure
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{{STRUCTURE_7pti| PDB=7pti | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=7pti FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pti OCA], [http://www.ebi.ac.uk/pdbsum/7pti PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=7pti RCSB]</span>
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'''STRUCTURAL EFFECTS INDUCED BY REMOVAL OF A DISULFIDE BRIDGE. THE X-RAY STRUCTURE OF THE C30A(SLASH)C51A MUTANT OF BASIC PANCREATIC TRYPSIN INHIBITOR AT 1.6 ANGSTROMS'''
'''STRUCTURAL EFFECTS INDUCED BY REMOVAL OF A DISULFIDE BRIDGE. THE X-RAY STRUCTURE OF THE C30A(SLASH)C51A MUTANT OF BASIC PANCREATIC TRYPSIN INHIBITOR AT 1.6 ANGSTROMS'''
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[[Category: Kossiakoff, A A.]]
[[Category: Kossiakoff, A A.]]
[[Category: Randal, M.]]
[[Category: Randal, M.]]
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[[Category: proteinase inhibitor (trypsin)]]
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Revision as of 19:47, 4 May 2008

Template:STRUCTURE 7pti

STRUCTURAL EFFECTS INDUCED BY REMOVAL OF A DISULFIDE BRIDGE. THE X-RAY STRUCTURE OF THE C30A(SLASH)C51A MUTANT OF BASIC PANCREATIC TRYPSIN INHIBITOR AT 1.6 ANGSTROMS


Overview

The X-ray structure of a variant of basic pancreatic trypsin inhibitor (BPTI) has been analyzed to determine the structural accommodation resulting from removal of a disulfide cross-link in a protein. The disulfide removed, Cys30-Cys51, has been implicated in both the folding pathway of the protein and its overall thermal stability. In the variant studied, C30A/C51A, the disulfide cysteines were replaced by less bulky alanines. The atomic displacements observed for C30A/C51A indicate a set of concerted shifts of two segments of chains, which together significantly diminish a packing defect at the site of the removed cysteine sulfur atoms. The observed structural changes are distributed asymmetrically around the sites of mutation, indicating that the adjacent beta-sheet is more resistant to the perturbation than the alpha-helix on the opposite side of the disulfide bond. The thermal parameters of groups involved in the structural accommodation are not significantly altered. A comparison of the X-ray structures reported for native BPTI determined in three different crystal forms indicates that the magnitude of its conformational variability exceeds that of the structural changes caused by the disulfide removal. This emphasizes the necessity of using isomorphous crystal systems to determine the relatively small effects due to mutation.

About this Structure

7PTI is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

Structural effects induced by removal of a disulfide-bridge: the X-ray structure of the C30A/C51A mutant of basic pancreatic trypsin inhibitor at 1.6 A., Eigenbrot C, Randal M, Kossiakoff AA, Protein Eng. 1990 Jul;3(7):591-8. PMID:1699222 Page seeded by OCA on Sun May 4 22:47:23 2008

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