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New page: left|200px<br /><applet load="1aug" size="450" color="white" frame="true" align="right" spinBox="true" caption="1aug, resolution 2.0Å" /> '''CRYSTAL STRUCTURE OF ...
 
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[[Image:1aug.gif|left|200px]]<br /><applet load="1aug" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1aug, resolution 2.0&Aring;" />
'''CRYSTAL STRUCTURE OF THE PYROGLUTAMYL PEPTIDASE I FROM BACILLUS AMYLOLIQUEFACIENS'''<br />


==Overview==
==CRYSTAL STRUCTURE OF THE PYROGLUTAMYL PEPTIDASE I FROM BACILLUS AMYLOLIQUEFACIENS==
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.
<StructureSection load='1aug' size='340' side='right'caption='[[1aug]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1aug]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AUG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AUG FirstGlance]. <br>
1AUG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]. 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=1AUG OCA].
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
 
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1aug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aug OCA], [https://pdbe.org/1aug PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aug RCSB], [https://www.ebi.ac.uk/pdbsum/1aug PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aug ProSAT]</span></td></tr>
==Reference==
</table>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10196127 10196127]
== Function ==
[https://www.uniprot.org/uniprot/PCP_BACAM PCP_BACAM] Removes 5-oxoproline from various penultimate amino acid residues except L-proline.[HAMAP-Rule:MF_00417]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/au/1aug_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1aug ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Bacillus amyloliquefaciens]]
[[Category: Bacillus amyloliquefaciens]]
[[Category: Pyroglutamyl-peptidase I]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Clardy J]]
[[Category: Clardy, J.]]
[[Category: Hayashi A]]
[[Category: Hayashi, A.]]
[[Category: Hirotsu K]]
[[Category: Hirotsu, K.]]
[[Category: Ito K]]
[[Category: Ito, K.]]
[[Category: Kabashima T]]
[[Category: Kabashima, T.]]
[[Category: Odagaki Y]]
[[Category: Odagaki, Y.]]
[[Category: Okada K]]
[[Category: Okada, K.]]
[[Category: Sato M]]
[[Category: Sato, M.]]
[[Category: Tsuru D]]
[[Category: Tsuru, D.]]
[[Category: Yoshimoto T]]
[[Category: Yoshimoto, T.]]
[[Category: bacillus amyloliquefaciens]]
[[Category: cysteine proteinase]]
[[Category: hydrolase]]
[[Category: pyroglutamyl peptidase]]
[[Category: thiol protease]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:08:18 2007''

Latest revision as of 06:33, 7 February 2024

CRYSTAL STRUCTURE OF THE PYROGLUTAMYL PEPTIDASE I FROM BACILLUS AMYLOLIQUEFACIENS

1aug, resolution 2.00Å

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