3m7q: Difference between revisions
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==Crystal structure of recombinant Kunitz Type serine protease Inhibitor-1 from the Caribbean sea anemone stichodactyla helianthus in complex with bovine pancreatic trypsin== | ==Crystal structure of recombinant Kunitz Type serine protease Inhibitor-1 from the Caribbean sea anemone stichodactyla helianthus in complex with bovine pancreatic trypsin== | ||
<StructureSection load='3m7q' size='340' side='right' caption='[[3m7q]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='3m7q' size='340' side='right'caption='[[3m7q]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3m7q]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Stihl Stihl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M7Q OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[3m7q]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Stihl Stihl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M7Q OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3M7Q FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3m7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m7q OCA], [http://pdbe.org/3m7q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3m7q RCSB], [http://www.ebi.ac.uk/pdbsum/3m7q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3m7q ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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==See Also== | ==See Also== | ||
*[[Trypsin|Trypsin]] | *[[Trypsin 3D structures|Trypsin 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Large Structures]] | |||
[[Category: Stihl]] | [[Category: Stihl]] | ||
[[Category: Trypsin]] | [[Category: Trypsin]] | ||
Revision as of 09:40, 14 October 2020
Crystal structure of recombinant Kunitz Type serine protease Inhibitor-1 from the Caribbean sea anemone stichodactyla helianthus in complex with bovine pancreatic trypsinCrystal structure of recombinant Kunitz Type serine protease Inhibitor-1 from the Caribbean sea anemone stichodactyla helianthus in complex with bovine pancreatic trypsin
Structural highlights
Function[ISH1_STOHE] Active against serine, cysteine, and aspartic proteinases. Can bind vertebrate trypsin and chymotrypsin.[1] [2] Publication Abstract from PubMedProteins isolated from marine invertebrates are frequently characterized by exceptional structural and functional properties. ShPI-1, a BPTI Kunitz-type inhibitor from the Caribbean Sea anemone Stichodactyla helianthus, displays activity not only against serine-, but also against cysteine-, and aspartate proteases. As an initial step to evaluate the molecular basis of its activities, we describe the crystallographic structure of ShPI-1 in complex with the serine protease bovine pancreatic trypsin at 1.7A resolution. The overall structure and the important enzyme-inhibitor interactions of this first invertebrate BPTI-like Kunitz-type inhibitor:trypsin complex remained largely conserved compared to mammalian BPTI-Kunitz inhibitor complexes. However, a prominent stabilizing role within the interface was attributed to arginine at position P3. Binding free-energy calculations indicated a 10-fold decrease for the inhibitor affinity against trypsin, if the P3 residue of ShPI-1 is mutated to alanine. Together with the increased role of Arg(11) at P3 position, slightly reduced interactions at the prime side (Pn') of the primary binding loop and at the secondary binding loop of ShPI-1 were detected. In addition, the structure provides important information for site directed mutagenesis to further optimize the activity of rShPI-1A for biotechnological applications. Structural insights into serine protease inhibition by a marine invertebrate BPTI Kunitz-type inhibitor.,Garcia-Fernandez R, Pons T, Perbandt M, Valiente PA, Talavera A, Gonzalez-Gonzalez Y, Rehders D, Chavez MA, Betzel C, Redecke L J Struct Biol. 2012 Sep 5. pii: S1047-8477(12)00240-7. doi:, 10.1016/j.jsb.2012.08.009. PMID:22975140[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Bos taurus
- Large Structures
- Stihl
- Trypsin
- Betzel, C
- Chavez, M de los angeles
- Garcia-Fernandez, R
- Gil, D
- Gonzalez, Y
- Perbandt, M
- Pons, T
- Redecke, L
- Talavera, A
- Digestion
- Disulfide bond
- Hydrolase
- Hydrolase-hydrolase inhibitor complex
- Kunitz-type serine-protease inhibitor
- Metal-binding
- Nematocyst
- Protease
- Protease inhibitor
- Secreted
- Serine protease
- Serine protease inhibitor
- Trypsin-inhibitor complex
- Zymogen