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1iu8
From Proteopedia
(New page: 200px<br /><applet load="1iu8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iu8, resolution 1.60Å" /> '''The X-ray Crystal St...) |
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| - | [[Image:1iu8.jpg|left|200px]]<br /><applet load="1iu8" size=" | + | [[Image:1iu8.jpg|left|200px]]<br /><applet load="1iu8" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1iu8, resolution 1.60Å" /> | caption="1iu8, resolution 1.60Å" /> | ||
'''The X-ray Crystal Structure of Pyrrolidone-Carboxylate Peptidase from Hyperthermophilic Archaeon Pyrococcus horikoshii'''<br /> | '''The X-ray Crystal Structure of Pyrrolidone-Carboxylate Peptidase from Hyperthermophilic Archaeon Pyrococcus horikoshii'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of pyrrolidone-carboxylate peptidase (PCP) from | + | The crystal structure of pyrrolidone-carboxylate peptidase (PCP) from hyperthermophilic archaea Pyrococcus horikoshii (PhoPCP) has been determined at 1.6-A resolution by X-ray crystallography. PCP belongs to the C15 family of cysteine protease, and specifically removes the amino terminal pyroglutamate residue from a wide range of N-terminal-blocking peptides. The crystal structure is very similar to that of other hyperthermophiles, Pyrococcus furiosus and Thermococcus litoralis, and even that from the mesophile, Bacillus amyloliquefaciens. The inter-subunit disulfide bonds, which have been proposed as one of the thermostabilizing factors of the PCP from such hyperthermophiles, was not present in PhoPCP. The result suggests that the thermostability of PhoPCP may be obtained by the accumulation of many weak factors. |
==About this Structure== | ==About this Structure== | ||
| - | 1IU8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Active as [http://en.wikipedia.org/wiki/Pyroglutamyl-peptidase_I Pyroglutamyl-peptidase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.3 3.4.19.3] Full crystallographic information is available from [http:// | + | 1IU8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Active as [http://en.wikipedia.org/wiki/Pyroglutamyl-peptidase_I Pyroglutamyl-peptidase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.3 3.4.19.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IU8 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: thiol protease]] | [[Category: thiol protease]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:15:41 2008'' |
Revision as of 11:15, 21 February 2008
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The X-ray Crystal Structure of Pyrrolidone-Carboxylate Peptidase from Hyperthermophilic Archaeon Pyrococcus horikoshii
Overview
The crystal structure of pyrrolidone-carboxylate peptidase (PCP) from hyperthermophilic archaea Pyrococcus horikoshii (PhoPCP) has been determined at 1.6-A resolution by X-ray crystallography. PCP belongs to the C15 family of cysteine protease, and specifically removes the amino terminal pyroglutamate residue from a wide range of N-terminal-blocking peptides. The crystal structure is very similar to that of other hyperthermophiles, Pyrococcus furiosus and Thermococcus litoralis, and even that from the mesophile, Bacillus amyloliquefaciens. The inter-subunit disulfide bonds, which have been proposed as one of the thermostabilizing factors of the PCP from such hyperthermophiles, was not present in PhoPCP. The result suggests that the thermostability of PhoPCP may be obtained by the accumulation of many weak factors.
About this Structure
1IU8 is a Single protein structure of sequence from Pyrococcus horikoshii. Active as Pyroglutamyl-peptidase I, with EC number 3.4.19.3 Full crystallographic information is available from OCA.
Reference
The X-ray crystal structure of pyrrolidone-carboxylate peptidase from hyperthermophilic archaea Pyrococcus horikoshii., Sokabe M, Kawamura T, Sakai N, Yao M, Watanabe N, Tanaka I, J Struct Funct Genomics. 2002;2(3):145-54. PMID:12836705
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