1gkt
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NEUTRON LAUE DIFFRACTION STRUCTURE OF ENDOTHIAPEPSIN COMPLEXED WITH TRANSITION STATE ANALOGUE INHIBITOR H261
OverviewOverview
Current proposals for the catalytic mechanism of aspartic proteinases are, largely based on X-ray structures of bound oligopeptide inhibitors, possessing nonhydrolyzable analogues of the scissile peptide bond., However, the positions of protons on the catalytic aspartates and the, ligand in these complexes have not been determined with certainty. Thus, our objective was to locate crucial protons at the active site of an, inhibitor complex since this will have major implications for a detailed, understanding of the mechanism of action. We have demonstrated that, high-resolution neutron diffraction data can be collected from crystals of, the fungal aspartic proteinase endothiapepsin bound to a transition state, analogue (H261). The neutron structure of the complex has been refined at, a ... [(full description)]
About this StructureAbout this Structure
1GKT is a [Protein complex] structure of sequences from [Cryphonectria parasitica]. Active as [Hydrolase], with EC number [3.4.23.22]. Structure known Active Site: CAT. Full crystallographic information is available from [OCA].
ReferenceReference
A neutron Laue diffraction study of endothiapepsin: implications for the aspartic proteinase mechanism., Coates L, Erskine PT, Wood SP, Myles DA, Cooper JB, Biochemistry. 2001 Nov 6;40(44):13149-57. PMID:11683623
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