1x9y

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(New page: 200px<br /><applet load="1x9y" size="450" color="white" frame="true" align="right" spinBox="true" caption="1x9y, resolution 2.50&Aring;" /> '''The prostaphopain B ...)
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[[Image:1x9y.gif|left|200px]]<br /><applet load="1x9y" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1x9y, resolution 2.50&Aring;" />
caption="1x9y, resolution 2.50&Aring;" />
'''The prostaphopain B structure'''<br />
'''The prostaphopain B structure'''<br />
==Overview==
==Overview==
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Prostaphopain B is the precursor of staphopain B, a papain-type secreted, cysteine protease from the pathogen Staphylococcus aureus. Here, we, describe the 2.5 A crystal structure of the proenzyme. Its 21 kDa, proregion is organized around a central half-barrel or barrel-sandwich, hybrid and occludes primed, but not nonprimed, sites in the active site, cleft of the protease. The structure of the mature part of the protease is, similar to previously reported staphopain structures, and no distortion of, the catalytic residues is apparent at 2.5 A resolution. A comparison of, prostaphopain B with the staphopain B-staphostatin B complex shows that, the proregion and the inhibitor interact with largely nonoverlapping parts, of the protease surface. In a modeled complex of prostaphopain B with, staphostatin B, clashes occur both inside and outside the active site, cleft, but involve mostly poorly ordered regions of the protein that may, be mobile.
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Prostaphopain B is the precursor of staphopain B, a papain-type secreted cysteine protease from the pathogen Staphylococcus aureus. Here, we describe the 2.5 A crystal structure of the proenzyme. Its 21 kDa proregion is organized around a central half-barrel or barrel-sandwich hybrid and occludes primed, but not nonprimed, sites in the active site cleft of the protease. The structure of the mature part of the protease is similar to previously reported staphopain structures, and no distortion of the catalytic residues is apparent at 2.5 A resolution. A comparison of prostaphopain B with the staphopain B-staphostatin B complex shows that the proregion and the inhibitor interact with largely nonoverlapping parts of the protease surface. In a modeled complex of prostaphopain B with staphostatin B, clashes occur both inside and outside the active site cleft, but involve mostly poorly ordered regions of the protein that may be mobile.
==About this Structure==
==About this Structure==
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1X9Y is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1X9Y OCA].
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1X9Y is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X9Y OCA].
==Reference==
==Reference==
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[[Category: half-barrel]]
[[Category: half-barrel]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:55:39 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:52:35 2008''

Revision as of 13:52, 21 February 2008


1x9y, resolution 2.50Å

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The prostaphopain B structure

Overview

Prostaphopain B is the precursor of staphopain B, a papain-type secreted cysteine protease from the pathogen Staphylococcus aureus. Here, we describe the 2.5 A crystal structure of the proenzyme. Its 21 kDa proregion is organized around a central half-barrel or barrel-sandwich hybrid and occludes primed, but not nonprimed, sites in the active site cleft of the protease. The structure of the mature part of the protease is similar to previously reported staphopain structures, and no distortion of the catalytic residues is apparent at 2.5 A resolution. A comparison of prostaphopain B with the staphopain B-staphostatin B complex shows that the proregion and the inhibitor interact with largely nonoverlapping parts of the protease surface. In a modeled complex of prostaphopain B with staphostatin B, clashes occur both inside and outside the active site cleft, but involve mostly poorly ordered regions of the protein that may be mobile.

About this Structure

1X9Y is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.

Reference

Prostaphopain B structure: a comparison of proregion-mediated and staphostatin-mediated protease inhibition., Filipek R, Szczepanowski R, Sabat A, Potempa J, Bochtler M, Biochemistry. 2004 Nov 9;43(44):14306-15. PMID:15518582

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