Document Detail


Structure of native porcine pancreatic elastase at 1.65 A resolutions.
MedLine Citation:
PMID:  3271103     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The structure of native porcine pancreatic elastase in 70% methanol has been refined using film data to 1.65 A resolution, R = 0.169. A total of 134 molecules of water (but no methanol) has been refined. This structure, because of its native state and modestly high resolution, serves as the basis for comparison with other elastase structures complexed with natural or synthetic ligands. Internal structured water occupies distinct regions. Two regions (IW1 and IW7) suggest a mechanism for equalizing 'hydrostatic pressure' related to ligand binding and release. A third region (IW4) forms part of a hydrogen-bonding network linking the catalytic Ser 195 O gamma with a remote (13.4 A) surface of the enzyme. A comparison with the structures of all known serine proteases reveals that a linkage of Ser O gamma to remote surface is conserved in all cases, suggesting that the accepted catalytic mechanism of serine proteases needs to be re-evaluated. One possible mechanism for base catalysis of Ser O gamma H proton extraction is presented.
Authors:
E Meyer; G Cole; R Radhakrishnan; O Epp
Related Documents :
7933803 - Relative roles of elastase and reactive oxygen species in the degradation of human glom...
1715763 - Neutrophil proteases in plasminogen activation.
10679523 - Production of an activated form of bacillus stearothermophilus l-2-hydroxyacid dehydrog...
Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.    
Journal Detail:
Title:  Acta crystallographica. Section B, Structural science     Volume:  44 ( Pt 1)     ISSN:  0108-7681     ISO Abbreviation:  Acta Crystallogr., B     Publication Date:  1988 Feb 
Date Detail:
Created Date:  1990-03-01     Completed Date:  1990-03-01     Revised Date:  2007-07-24    
Medline Journal Info:
Nlm Unique ID:  8403252     Medline TA:  Acta Crystallogr B     Country:  DENMARK    
Other Details:
Languages:  eng     Pagination:  26-38     Citation Subset:  IM    
Affiliation:
Department of Biochemistry and Biophysics, Texas A&M University, College Station 77843-2128.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Animals
Binding Sites
Calcium / metabolism
Crystallography
Hydrogen Bonding
Molecular Structure
Pancreatic Elastase* / analysis
Protein Conformation
Structure-Activity Relationship
Swine
Temperature
Water / analysis
Chemical
Reg. No./Substance:
7440-70-2/Calcium; 7732-18-5/Water; EC 3.4.21.36/Pancreatic Elastase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Cryocrystallography of biological macromolecules: a generally applicable method.
Next Document:  More space-group changes.