3aho

<table><tr><td colspan='2'>[[3aho]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Geobacillus_sp._mo-1 Geobacillus sp. mo-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AHO OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3AHO FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3A2:1-{3-[(R)-{(1R)-1-[(GLYCYL-L-PROLYL)AMINO]-2-PHENYLETHYL}(HYDROXY)PHOSPHORYL]PROPANOYL}-L-PROLYL-D-NORLEUCINE'>3A2</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ahm|3ahm]], [[3ahn|3ahn]]</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3aho FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aho OCA], [http://pdbe.org/3aho PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3aho RCSB], [http://www.ebi.ac.uk/pdbsum/3aho PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3aho ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Pz-peptidase A, from the thermophilic bacterium Geobacillus collagenovorans MO-1, hydrolyzes a synthetic peptide substrate, 4-phenylazobenzyloxycarbonyl-Pro-Leu-Gly-Pro-D-Arg (Pz-PLGPR), which contains a collagen-specific tripeptide sequence, -Gly-Pro-X-, but does not act on collagen proteins themselves. The mammalian enzyme, thimet oligopeptidase (TOP), which has comparable functions with bacterial Pz-peptidases but limited identity at the primary sequence level, has recently been subjected to x-ray crystallographic analysis; however, no crystal structure has yet been reported for complexes of TOP with substrate analogues. Here, we report crystallization of recombinant Pz-peptidase A in complex with two phosphinic peptide inhibitors (PPIs) that also function as inhibitors of TOP and determination of the crystal structure of these complexes at 1.80-2.00 A resolution. The most striking difference between Pz-peptidase A and TOP is that there is no channel running the length of bacterial protein. Whereas the structure of TOP resembles an open bivalve, that of Pz-peptidase A is closed and globular. This suggests that collagenous peptide substrates enter the tunnel at the top gateway of the closed Pz-peptidase A molecule, and reactant peptides are released from the bottom gateway after cleavage at the active site located in the center of the tunnel. One of the two PPIs, PPI-2, which contains the collagen-specific sequence, helped to clarify the exquisite structure and reaction mechanism of Pz-peptidase A toward collagenous peptides. This study describes the mode of substrate binding and its implication for the mammalian enzymes.

The exquisite structure and reaction mechanism of bacterial Pz-peptidase A toward collagenous peptides: X-ray crystallographic structure analysis of PZ-peptidase a reveals differences from mammalian thimet oligopeptidase.,Kawasaki A, Nakano H, Hosokawa A, Nakatsu T, Kato H, Watanabe K J Biol Chem. 2010 Nov 5;285(45):34972-80. Epub 2010 Sep 3. PMID:20817732<ref>PMID:20817732</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Geobacillus sp. mo-1]]

[[Category: Nakano, H]]

[[Category: Hydrolase-hydrolase inhibitor complex]]