1iu8

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1iu8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iu8, resolution 1.60&Aring;" /> '''The X-ray Crystal St...)
Line 1: Line 1:
-
[[Image:1iu8.jpg|left|200px]]<br /><applet load="1iu8" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1iu8.jpg|left|200px]]<br /><applet load="1iu8" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1iu8, resolution 1.60&Aring;" />
caption="1iu8, resolution 1.60&Aring;" />
'''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, 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.
+
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IU8 OCA].
+
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==
Line 24: Line 24:
[[Category: thiol protease]]
[[Category: thiol protease]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:40:20 2007''
+
''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


1iu8, resolution 1.60Å

Drag the structure with the mouse to rotate

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

Page seeded by OCA on Thu Feb 21 13:15:41 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools