1a2z
From Proteopedia
(New page: 200px<br /> <applet load="1a2z" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a2z, resolution 1.73Å" /> '''PYRROLIDONE CARBOXY...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1A2Z is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Thermococcus_litoralis Thermococcus litoralis]] with SO4 as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], 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=1A2Z OCA]]. | + | 1A2Z is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Thermococcus_litoralis Thermococcus litoralis]] with SO4 as [[http://en.wikipedia.org/wiki/ligand ligand]]. 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]]. Structure known Active Site: AVE. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1A2Z OCA]]. |
==Reference== | ==Reference== | ||
X-ray structure of pyrrolidone carboxyl peptidase from the hyperthermophilic archaeon Thermococcus litoralis., Singleton M, Isupov M, Littlechild J, Structure. 1999 Mar 15;7(3):237-44. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10368293 10368293] | X-ray structure of pyrrolidone carboxyl peptidase from the hyperthermophilic archaeon Thermococcus litoralis., Singleton M, Isupov M, Littlechild J, Structure. 1999 Mar 15;7(3):237-44. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10368293 10368293] | ||
| + | [[Category: Pyroglutamyl-peptidase I]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermococcus litoralis]] | [[Category: Thermococcus litoralis]] | ||
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[[Category: peptidase]] | [[Category: peptidase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:08:13 2007'' |
Revision as of 10:03, 30 October 2007
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PYRROLIDONE CARBOXYL PEPTIDASE FROM THERMOCOCCUS LITORALIS
Overview
BACKGROUND: Pyrrolidone carboxyl peptidases (pcps) are a group of, exopeptidases responsible for the hydrolysis of N-terminal pyroglutamate, residues from peptides and proteins. The bacterial and archaeal pcps are, members of a conserved family of cysteine proteases. The pcp from the, hyperthermophilic archaeon Thermococcus litoralis is more thermostable, than the bacterial enzymes with which it has up to 40% sequence identity., The pcp activity in archaea and eubacteria is proposed to be involved in, detoxification processes and in nutrient metabolism; eukaryotic, counterparts of the enzyme are involved in the processing of biologically, active peptides. RESULTS: The crystal structure of pcp has been determined, by multiple isomorphous replacement techniques at 1.73 A resolution and, ... [(full description)]
About this Structure
1A2Z is a [Single protein] structure of sequence from [Thermococcus litoralis] with SO4 as [ligand]. Active as [Pyroglutamyl-peptidase I], with EC number [3.4.19.3]. Structure known Active Site: AVE. Full crystallographic information is available from [OCA].
Reference
X-ray structure of pyrrolidone carboxyl peptidase from the hyperthermophilic archaeon Thermococcus litoralis., Singleton M, Isupov M, Littlechild J, Structure. 1999 Mar 15;7(3):237-44. PMID:10368293
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