3apr

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(New page: 200px<br /><applet load="3apr" size="450" color="white" frame="true" align="right" spinBox="true" caption="3apr, resolution 1.8&Aring;" /> '''BINDING OF A REDUCED ...)
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caption="3apr, resolution 1.8&Aring;" />
'''BINDING OF A REDUCED PEPTIDE INHIBITOR TO THE ASPARTIC PROTEINASE FROM RHIZOPUS CHINENSIS. IMPLICATIONS FOR A MECHANISM OF ACTION'''<br />
'''BINDING OF A REDUCED PEPTIDE INHIBITOR TO THE ASPARTIC PROTEINASE FROM RHIZOPUS CHINENSIS. IMPLICATIONS FOR A MECHANISM OF ACTION'''<br />
==Overview==
==Overview==
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A peptide inhibitor, having the sequence D-His-Pro-Phe-His-Phe psi, [CH2-NH]Phe-Val-Tyr, with a reduced bond between the two adjacent, phenylalanines, has been diffused into crystals of the aspartic proteinase, from Rhizopus chinensis (rhizopuspepsin, EC 3.4.23.6). X-ray diffraction, data to 1.8-A resolution have been collected on the complex, which has, been subjected to restrained least-squares refinement to an R-factor (R, equals the sum of the absolute value of the difference between the, observed and calculated structure factor amplitudes divided by the sum of, the observed structure factor amplitudes) of 14.7%. The inhibitor lies, within the major groove of the enzyme and is clearly defined with the, exception of the amino-terminal D-histidine and the carboxyl-terminal, tyrosine. The reduced peptide bond is located in the active site with, close contacts to the two catalytic aspartyl groups. The active-site water, molecule that is held between the two carboxyl groups is displaced by the, inhibitor, as are a number of other water molecules seen in the binding, groove of the native enzyme. A mechanism of action for this class of, enzymes is proposed from these results.
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A peptide inhibitor, having the sequence D-His-Pro-Phe-His-Phe psi [CH2-NH]Phe-Val-Tyr, with a reduced bond between the two adjacent phenylalanines, has been diffused into crystals of the aspartic proteinase from Rhizopus chinensis (rhizopuspepsin, EC 3.4.23.6). X-ray diffraction data to 1.8-A resolution have been collected on the complex, which has been subjected to restrained least-squares refinement to an R-factor (R equals the sum of the absolute value of the difference between the observed and calculated structure factor amplitudes divided by the sum of the observed structure factor amplitudes) of 14.7%. The inhibitor lies within the major groove of the enzyme and is clearly defined with the exception of the amino-terminal D-histidine and the carboxyl-terminal tyrosine. The reduced peptide bond is located in the active site with close contacts to the two catalytic aspartyl groups. The active-site water molecule that is held between the two carboxyl groups is displaced by the inhibitor, as are a number of other water molecules seen in the binding groove of the native enzyme. A mechanism of action for this class of enzymes is proposed from these results.
==About this Structure==
==About this Structure==
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3APR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Active as [http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.103, 3.4.23.18, 3.4.23.28 and 3.4.23.30 3.4.21.103, 3.4.23.18, 3.4.23.28 and 3.4.23.30] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=3APR OCA].
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3APR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Active as [http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.103, 3.4.23.18, 3.4.23.28 and 3.4.23.30 3.4.21.103, 3.4.23.18, 3.4.23.28 and 3.4.23.30] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3APR OCA].
==Reference==
==Reference==
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[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Davies, D.R.]]
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[[Category: Davies, D R.]]
[[Category: Suguna, K.]]
[[Category: Suguna, K.]]
[[Category: hydrolase (aspartic proteinase)]]
[[Category: hydrolase (aspartic proteinase)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:24:56 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:02:50 2008''

Revision as of 17:02, 21 February 2008


3apr, resolution 1.8Å

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BINDING OF A REDUCED PEPTIDE INHIBITOR TO THE ASPARTIC PROTEINASE FROM RHIZOPUS CHINENSIS. IMPLICATIONS FOR A MECHANISM OF ACTION

Overview

A peptide inhibitor, having the sequence D-His-Pro-Phe-His-Phe psi [CH2-NH]Phe-Val-Tyr, with a reduced bond between the two adjacent phenylalanines, has been diffused into crystals of the aspartic proteinase from Rhizopus chinensis (rhizopuspepsin, EC 3.4.23.6). X-ray diffraction data to 1.8-A resolution have been collected on the complex, which has been subjected to restrained least-squares refinement to an R-factor (R equals the sum of the absolute value of the difference between the observed and calculated structure factor amplitudes divided by the sum of the observed structure factor amplitudes) of 14.7%. The inhibitor lies within the major groove of the enzyme and is clearly defined with the exception of the amino-terminal D-histidine and the carboxyl-terminal tyrosine. The reduced peptide bond is located in the active site with close contacts to the two catalytic aspartyl groups. The active-site water molecule that is held between the two carboxyl groups is displaced by the inhibitor, as are a number of other water molecules seen in the binding groove of the native enzyme. A mechanism of action for this class of enzymes is proposed from these results.

About this Structure

3APR is a Single protein structure of sequence from [1]. Active as Hydrolase, with EC number 3.4.23.18, 3.4.23.28 and 3.4.23.30 3.4.21.103, 3.4.23.18, 3.4.23.28 and 3.4.23.30 Full crystallographic information is available from OCA.

Reference

Binding of a reduced peptide inhibitor to the aspartic proteinase from Rhizopus chinensis: implications for a mechanism of action., Suguna K, Padlan EA, Smith CW, Carlson WD, Davies DR, Proc Natl Acad Sci U S A. 1987 Oct;84(20):7009-13. PMID:3313384

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