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The structure of endothiapepsin complexed with the gem-diol inhibitor PD-135,040 at 1.37 angstrom

The structure of endothiapepsin complexed with the gem-diol inhibitor PD-135,040 at 1.37 angstrom
The structure of endothiapepsin complexed with the gem-diol inhibitor PD-135,040 at 1.37 angstrom
The crystal structure of endothiapepsin complexed with the gem-diol inhibitor PD-135,040 has been anisotropically refined to a resolution of 1.37 Å. The structure of this inhibitor complex is in agreement with previous structures of endothiapepsin gem-diol inhibitor complexes that have been used to develop proposed catalytic mechanisms. However, the increase in resolution over previous structures confirms the presence of a number of short hydrogen bonds within the active site that are likely to play an important role in the catalytic mechanism. The presence of low-barrier hydrogen bonds was indicated in a previous one-dimensional H NMR spectrum.
0907-4449
978-981
Coates, L.
2be36c11-8cb2-4518-a001-953051aa6a23
Erskine, P.T.
c77b60c5-b80c-4e6a-a103-bf57ecfcbcf6
Mall, S.
343a3062-0630-4e15-8d55-ebb4288f3a8b
Williams, P.A.
18f55b81-ad5c-4db1-892a-9bdcc5092a6b
Gill, R.S.
fbd80a07-b8b8-43ef-aa5c-926cec6e2bbf
Wood, S.P.
430faabf-7f5c-4cf6-9bcc-5955f5e09566
Cooper, J.B.
d9f0f6a8-1260-48fc-aa5c-3dbc650e3ec0
Coates, L.
2be36c11-8cb2-4518-a001-953051aa6a23
Erskine, P.T.
c77b60c5-b80c-4e6a-a103-bf57ecfcbcf6
Mall, S.
343a3062-0630-4e15-8d55-ebb4288f3a8b
Williams, P.A.
18f55b81-ad5c-4db1-892a-9bdcc5092a6b
Gill, R.S.
fbd80a07-b8b8-43ef-aa5c-926cec6e2bbf
Wood, S.P.
430faabf-7f5c-4cf6-9bcc-5955f5e09566
Cooper, J.B.
d9f0f6a8-1260-48fc-aa5c-3dbc650e3ec0

Coates, L., Erskine, P.T., Mall, S., Williams, P.A., Gill, R.S., Wood, S.P. and Cooper, J.B. (2003) The structure of endothiapepsin complexed with the gem-diol inhibitor PD-135,040 at 1.37 angstrom. Acta Crystallographica Section D: Biological Crystallography, 59 (6), 978-981. (doi:10.1107/S0907444903006267).

Record type: Article

Abstract

The crystal structure of endothiapepsin complexed with the gem-diol inhibitor PD-135,040 has been anisotropically refined to a resolution of 1.37 Å. The structure of this inhibitor complex is in agreement with previous structures of endothiapepsin gem-diol inhibitor complexes that have been used to develop proposed catalytic mechanisms. However, the increase in resolution over previous structures confirms the presence of a number of short hydrogen bonds within the active site that are likely to play an important role in the catalytic mechanism. The presence of low-barrier hydrogen bonds was indicated in a previous one-dimensional H NMR spectrum.

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Published date: 1 June 2003

Identifiers

Local EPrints ID: 56799
URI: http://eprints.soton.ac.uk/id/eprint/56799
ISSN: 0907-4449
PURE UUID: 42afe8d2-e869-4d08-9139-b0ecb9b6d3e3

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Date deposited: 06 Aug 2008
Last modified: 08 Jan 2022 07:07

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Contributors

Author: L. Coates
Author: P.T. Erskine
Author: S. Mall
Author: P.A. Williams
Author: R.S. Gill
Author: S.P. Wood
Author: J.B. Cooper

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