1aug

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[[Image:1aug.gif|left|200px]]
[[Image:1aug.gif|left|200px]]
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{{Structure
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1aug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aug OCA], [http://www.ebi.ac.uk/pdbsum/1aug PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1aug RCSB]</span>
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'''CRYSTAL STRUCTURE OF THE PYROGLUTAMYL PEPTIDASE I FROM BACILLUS AMYLOLIQUEFACIENS'''
'''CRYSTAL STRUCTURE OF THE PYROGLUTAMYL PEPTIDASE I FROM BACILLUS AMYLOLIQUEFACIENS'''
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[[Category: Tsuru, D.]]
[[Category: Tsuru, D.]]
[[Category: Yoshimoto, T.]]
[[Category: Yoshimoto, T.]]
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[[Category: bacillus amyloliquefacien]]
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[[Category: Bacillus amyloliquefacien]]
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[[Category: cysteine proteinase]]
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[[Category: Cysteine proteinase]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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[[Category: pyroglutamyl peptidase]]
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[[Category: Pyroglutamyl peptidase]]
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[[Category: thiol protease]]
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[[Category: Thiol protease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:42:13 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:47:44 2008''
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Revision as of 07:42, 2 May 2008

Image:1aug.gif

Template:STRUCTURE 1aug

CRYSTAL STRUCTURE OF THE PYROGLUTAMYL PEPTIDASE I FROM BACILLUS AMYLOLIQUEFACIENS


Overview

BACKGROUND: The N-terminal pyroglutamyl (pGlu) residue of peptide hormones, such as thyrotropin-releasing hormone (TRH) and luteinizing hormone releasing hormone (LH-RH), confers resistance to proteolysis by conventional aminopeptidases. Specialized pyroglutamyl peptidases (PGPs) are able to cleave an N-terminal pyroglutamyl residue and thus control hormonal signals. Until now, no direct or homology-based three-dimensional structure was available for any PGP. RESULTS: The crystal structure of pyroglutamyl peptidase I (PGP-I) from Bacillus amyloliquefaciens has been determined to 1.6 A resolution. The crystallographic asymmetric unit of PGP-I is a tetramer of four identical monomers related by noncrystallographic 222 symmetry. The protein folds into an alpha/beta globular domain with a hydrophobic core consisting of a twisted beta sheet surrounded by five alpha helices. The structure allows the function of most of the conserved residues in the PGP-I family to be identified. The catalytic triad comprises Cys144, His168 and Glu81. CONCLUSIONS: The catalytic site does not have a conventional oxyanion hole, although Cys144, the sidechain of Arg91 and the dipole of an alpha helix could all stabilize a negative charge. The catalytic site has an S1 pocket lined with conserved hydrophobic residues to accommodate the pyroglutamyl residue. Aside from the S1 pocket, there is no clearly defined mainchain substrate-binding region, consistent with the lack of substrate specificity. Although the overall structure of PGP-I resembles some other alpha/beta twisted open-sheet structures, such as purine nucleoside phosphorylase and cutinase, there are important differences in the location and organization of the active-site residues. Thus, PGP-I belongs to a new family of cysteine proteases.

About this Structure

1AUG is a Single protein structure of sequence from Bacillus amyloliquefaciens. Full crystallographic information is available from OCA.

Reference

The crystal structure of pyroglutamyl peptidase I from Bacillus amyloliquefaciens reveals a new structure for a cysteine protease., Odagaki Y, Hayashi A, Okada K, Hirotsu K, Kabashima T, Ito K, Yoshimoto T, Tsuru D, Sato M, Clardy J, Structure. 1999 Apr 15;7(4):399-411. PMID:10196127 Page seeded by OCA on Fri May 2 10:42:13 2008

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