3qh1

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3qh1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_thermoproteolyticus Bacillus thermoproteolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QH1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QH1 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3qh1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_thermoproteolyticus Bacillus thermoproteolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QH1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QH1 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NX6:N-[(BENZYLOXY)CARBONYL]-L-ASPARTIC+ACID'>NX6</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3qgo|3qgo]], [[2tlx|2tlx]], [[4tmn|4tmn]], [[5tmn|5tmn]], [[6tmn|6tmn]], [[1thl|1thl]], [[3qh5|3qh5]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NX6:N-[(BENZYLOXY)CARBONYL]-L-ASPARTIC+ACID'>NX6</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Thermolysin Thermolysin], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.27 3.4.24.27] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3qh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qh1 OCA], [https://pdbe.org/3qh1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qh1 RCSB], [https://www.ebi.ac.uk/pdbsum/3qh1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qh1 ProSAT]</span></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=3qh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qh1 OCA], [https://pdbe.org/3qh1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qh1 RCSB], [https://www.ebi.ac.uk/pdbsum/3qh1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qh1 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/THER_BACTH THER_BACTH]] Extracellular zinc metalloprotease.
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[https://www.uniprot.org/uniprot/THER_BACTH THER_BACTH] Extracellular zinc metalloprotease.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Protease mediated peptide synthesis (PMPS) was first described in the 1930s but remains underexploited today. In most PMPS, the reaction equilibrium is shifted toward synthesis by the aqueous insolubility of product generated. Substrates and proteases are selected by trial and error, yields are modest, and reaction times are slow. Once implemented, however, PMPS reactions can be simple, environmentally benign, and readily scalable to a commercial level. We examined the PMPS of a precursor of the artificial sweetener aspartame, a multiton peptide synthesis catalyzed by the enzyme thermolysin. X-ray structures of thermolysin in complex with aspartame substrates separately, and after PMPS in a crystal, rationalize the reaction's substrate preferences and reveal an unexpected form of substrate inhibition that explains its sluggishness. Structure guided optimization of this and other PMPS reactions could expand the economic viability of commercial peptides beyond current high-potency, low-volume therapeutics, with substantial green chemistry advantages.
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Synthesis of Aspartame by Thermolysin: An X-ray Structural Study.,Birrane G, Bhyravbhatla B, Navia MA ACS Med Chem Lett. 2014 Apr 10;5(6):706-10. doi: 10.1021/ml500101z. eCollection, 2014 Jun 12. PMID:24944748<ref>PMID:24944748</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3qh1" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Thermolysin 3D structures|Thermolysin 3D structures]]
*[[Thermolysin 3D structures|Thermolysin 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus thermoproteolyticus]]
[[Category: Bacillus thermoproteolyticus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Thermolysin]]
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[[Category: Bhyravbhatla B]]
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[[Category: Bhyravbhatla, B]]
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[[Category: Birrane G]]
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[[Category: Birrane, G]]
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[[Category: Navia M]]
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[[Category: Navia, M]]
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[[Category: Hydrolase]]
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[[Category: Hydrolase-hydrolase inhibitor complex]]
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[[Category: Metalloproteinase]]
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[[Category: N-benzyloxycarbonyl-l-aspartic acid]]
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Current revision

Structure of Thermolysin in complex with N-benzyloxycarbonyl-L-aspartic acid

PDB ID 3qh1

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