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

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

doi:10.1107/S0907444903006267

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

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

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	978-981
Journal	Acta Crystallographica Section D Biological Crystallography
Volume	59
Issue number	6
DOIs	https://doi.org/10.1107/S0907444903006267
Publication status	Published - 1 Jun 2003

Keywords

aspartic proteinase mechanism
tetrahedral intermediate
anisotropic refinement

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10.1107/S0907444903006267

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title = "The structure of endothiapepsin complexed with the gem-diol inhibitor PD-135,040 at 1.37 {\AA}",

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 {\AA}. 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.",

keywords = "aspartic proteinase mechanism, tetrahedral intermediate, anisotropic refinement",

author = "L. Coates and Erskine, {P. T.} and S. Mall and Williams, {P. A.} and Gill, {R. S.} and Wood, {S. P.} and Cooper, {J. B.}",

year = "2003",

month = jun,

day = "1",

doi = "10.1107/S0907444903006267",

language = "English",

volume = "59",

pages = "978--981",

journal = "Acta Crystallographica Section D Biological Crystallography",

issn = "0907-4449",

publisher = "International Union of Crystallography",

number = "6",

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TY - JOUR

T1 - The structure of endothiapepsin complexed with the gem-diol inhibitor PD-135,040 at 1.37 Å

AU - Coates, L.

AU - Erskine, P. T.

AU - Mall, S.

AU - Williams, P. A.

AU - Gill, R. S.

AU - Wood, S. P.

AU - Cooper, J. B.

PY - 2003/6/1

Y1 - 2003/6/1

N2 - 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.

AB - 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.

KW - aspartic proteinase mechanism

KW - tetrahedral intermediate

KW - anisotropic refinement

U2 - 10.1107/S0907444903006267

DO - 10.1107/S0907444903006267

M3 - Article

SN - 0907-4449

VL - 59

SP - 978

EP - 981

JO - Acta Crystallographica Section D Biological Crystallography

JF - Acta Crystallographica Section D Biological Crystallography

IS - 6

ER -

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

Abstract

Keywords

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